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A’ Level Biology Notes
A compilation of my A’ level notes

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April 7, 2022
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Contents
Contents v
Lower Six 1
1 Cell Structure and Function 3

1.1 Objectives . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3
1.2 Microscopy . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3
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1.2.1 Microscope . . . optical microscope . . . . . . . . . . . . . . . . . . . 3
1.3 Plant and Animal Cells . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 6
1.3.1 Plant cells . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 6
1.3.2 Animal cells . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 6
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1.4 Organelles & functions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 7
1.4.1 Nucleus . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 9
1.4.2 Cytoplasm . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 10
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1.4.3 Endoplasmic reticulum . . . . . . . . . . . . . . . . . . . . . . . . . 10
1.4.4 Rough endoplasmic reticulum . . . . . . . . . . . . . . . . . . . . . 10
1.4.5 Smooth endoplasmic reticulum . . . . . . . . . . . . . . . . . . . . 11
1.4.6 Ribosomes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 11
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1.4.7 Golgi apparatus . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 12

1.4.8 Mitochondrion . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 12
1.4.9 Chloroplast . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 13
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1.4.10 Centriole . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 13
1.4.11 Cell membrane . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 13
1.5 Eukaryotic & Prokaryotic cells . . . . . . . . . . . . . . . . . . . . . . . . . 18
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1.5.1 Prokaryotic cells . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 18

1.6 Movement of substances into and out of cells . . . . . . . . . . . . . . . . . 20
1.6.1 Transport across membranes . . . . . . . . . . . . . . . . . . . . . . 20
1.6.2 Diffusion . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 21
1.6.3 Active transport . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 22
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1.6.4 Osmosis . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 22
1.6.5 Endocytosis & exocytosis . . . . . . . . . . . . . . . . . . . . . . . . 23
1.7 Questions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 24
2 Biological Molecules and Water 25

2.1 Objectives . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 25
2.2 Water . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 26
2.2.1 Biological significance . . . . . . . . . . . . . . . . . . . . . . . . . . 26
2.2.2 Functions of water . . . . . . . . . . . . . . . . . . . . . . . . . . . . 28
2.3 Carbohydrates . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 28
2.3.1 Monosaccharides . . . . . . . . . . . . . . . . . . . . . . . . . . . . 28
2.3.2 Disaccharides . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 29
2.3.3 Polysaccharides . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 30
2.3.4 Glycosidic bond . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 33
2.4 Lipids . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 34
2.4.1 Fatty acids . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 34
2.4.2 Triglycerides . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 35
2.4.3 Phospholipids . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 37
2.5 Proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 37
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2.5.1 Amino acids . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 37
2.5.2 Bonds in Proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . 38
2.5.3 Structure of proteins . . . . . . . . . . . . . . . . . . . . . . . . . . 41
2.6 Questions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 44
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3 Enzymes 45
3.1 Properties of enzymes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 46
3.2 Mechanisms of action/Mode of action . . . . . . . . . . . . . . . . . . . . 46
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3.2.1 Lock and key . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 46
3.2.2 Induced fit . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 47
3.3 Rate of enzyme activity . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 47
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3.3.1 Factors affecting rate of activity . . . . . . . . . . . . . . . . . . . . 47

3.3.2 Enzyme inhibitors . . . . . . . . . . . . . . . . . . . . . . . . . . . . 51
3.4 Questions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 53
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4 ATP & Photosynthesis 55

4.1 Objectives . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 55
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4.2 ATP . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 55
4.2.1 Uses of energy . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 55
4.2.2 ATP . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 56
4.3 Photosynthesis . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 58
4.3.1 Chloroplast . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 58
4.3.2 Chlorophyll . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 59
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4.3.3 Absorption & action spectra . . . . . . . . . . . . . . . . . . . . . . 60

4.3.4 Photosynthesis . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 61
4.3.5 Light-independent reactions/Calvin cycle . . . . . . . . . . . . . . 64
4.3.6 Limiting factors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 66
4.4 Questions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 67
5 Respiration 69
5.1 Objectives . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 69
5.2 Respiration . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 69
5.2.1 Mitochondrion . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 69
5.2.2 Glycolysis . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 70
5.2.3 Link reaction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 71
5.2.4 Krebs cycle . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 72
5.2.5 Electron Transport Chain . . . . . . . . . . . . . . . . . . . . . . . . 73
5.2.6 Anaerobic respiration . . . . . . . . . . . . . . . . . . . . . . . . . . 74
5.2.7 Energy values of different substrates . . . . . . . . . . . . . . . . . 75
5.2.8 Respiratory quotient . . . . . . . . . . . . . . . . . . . . . . . . . . 76
5.3 Questions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 76
6 Sexual Reproduction in plants 77

6.1 Objectives . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 77
6.2 Sexual Reproduction in Plants . . . . . . . . . . . . . . . . . . . . . . . . . 77
6.3 Development of pollen grains . . . . . . . . . . . . . . . . . . . . . . . . . 78
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6.4 Structure of ovule . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 79
6.4.1 Development of ovule . . . . . . . . . . . . . . . . . . . . . . . . . . 79
6.5 Double fertilisation . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 80
6.6 Questions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 81
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7 Transport in animals 83
7.1 Objectives . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 83
7.2 Mammalian circulatory system . . . . . . . . . . . . . . . . . . . . . . . . . 83
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7.3 Blood vessels . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 84
7.3.1 Arteries . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 84
7.3.2 Veins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 85
7.3.3 Capillaries . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 85
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7.4 Oxygen transport . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 85

7.4.1 Structure of haemoglobin . . . . . . . . . . . . . . . . . . . . . . . . 85
7.4.2 Structure of myoglobin & foetal haemoglobin . . . . . . . . . . . . 86
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7.4.3 Oxygen transport . . . . . . . . . . . . . . . . . . . . . . . . . . . . 87

7.4.4 Carbon dioxide transport . . . . . . . . . . . . . . . . . . . . . . . . 88
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7.4.5 Dissociation curve . . . . . . . . . . . . . . . . . . . . . . . . . . . . 89

7.5 Cardiac cycle . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 91
7.5.1 Myogenic stimulation of the heart . . . . . . . . . . . . . . . . . . . 94
7.5.2 Regulation of heart rate . . . . . . . . . . . . . . . . . . . . . . . . . 95
7.5.3 Exercise & cardiovascular system . . . . . . . . . . . . . . . . . . . 96
7.6 Questions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 97
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8 Cell and nuclear division 99

8.1 Objectives . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 99
8.2 Cell cycle . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 99
8.3 Mitosis . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 101
8.3.1 Interphase . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 101
8.3.2 Prophase . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 102
8.3.3 Metaphase . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 102
8.3.4 Anaphase . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 102
8.3.5 Telophase . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 103
8.4 Cytokinesis . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 103
8.4.1 Animal cells . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 103
8.4.2 Plant cell . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 104
8.4.3 Differences between mitosis in plants & animals cells . . . . . . . . 105
8.4.4 Importance of mitosis . . . . . . . . . . . . . . . . . . . . . . . . . . 105
8.4.5 Cancer . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 106
8.5 Meiosis . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 107
8.5.1 Meiosis I . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 108
8.5.2 Meiosis II . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 111
8.5.3 Significance of meiosis . . . . . . . . . . . . . . . . . . . . . . . . . 113
8.5.4 Mitosis and meiosis . . . . . . . . . . . . . . . . . . . . . . . . . . . 113
8.6 Questions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 114
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9 Genetic control 117
9.1 Objectives . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 117
9.2 Nucleic acid . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 117
9.2.1 Nucleotides . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 118
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9.2.2 Polynucleotides . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 119
9.3 Replication of DNA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 123
9.3.1 Protein synthesis . . . . . . . . . . . . . . . . . . . . . . . . . . . . 127
9.4 Questions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 133
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10 Inherited change & evolution 135
10.1 Objectives . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 135
10.2 Nature of genes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 135
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10.2.1 Genes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 135

10.2.2 The nature of genes . . . . . . . . . . . . . . . . . . . . . . . . . . . 136
10.3 Genetic crosses . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 136
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10.3.1 Monohybrid crosses . . . . . . . . . . . . . . . . . . . . . . . . . . . 136

10.3.2 Dihybrid crosses . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 143
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10.3.3 Chi squared tests . . . . . . . . . . . . . . . . . . . . . . . . . . . . 146

10.4 Questions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 150
11 Inherited change & evolution 153

11.1 Objectives . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 153
11.1.1 Variation . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 153
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11.2 Natural selection . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 154

11.2.1 Selection pressures & survival . . . . . . . . . . . . . . . . . . . . . 155
11.2.2 Stabilising, directional & disruptive selection . . . . . . . . . . . . 155
11.3 Artificial selection . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 157
11.3.1 Inbreeding . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 158
11.3.2 Outbreeding . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 158
11.4 Questions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 159
Upper Six 161

Appendix 163
Alphabetical Index 165
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List of Figures
1.1 Optical microscope . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4

1.2 Nucleus . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 9
1.3 Rough endoplasmic reticulum . . . . . . . . . . . . . . . . . . . . . . . . . . . 11
1.4 Ribosomes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 11
1.5 Golgi apparatus . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 12
1.6 Mitochondrion . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 12
1.7 Chloroplast . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 13
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1.8 Cetriole . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 13
1.9 Cell membrane . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 14
1.11 Prokaryotic cells . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 18
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1.12 Active transport . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 22
2.1 water . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 26
2.2 pentose . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 28
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2.3 Glucose isomers . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 29
2.4 disach . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 30
2.5 maltose . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 30
2.6 lactose . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 30
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2.7 sucrose . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 30
2.8 amylose . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 31
2.9 amylo . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 31
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2.10 amylopectin . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 32
2.11 amylop . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 32
2.12 cello . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 32
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2.13 cell . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 33
2.14 amylop . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 33
2.15 Condensation . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 33
2.16 fattyacid . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 34
2.17 glycerol . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 35
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2.18 Formation of triglycerides . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 36

2.19 Phospholipid . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 37
2.20 ATP . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 39
2.21 Acidic group. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 39
2.22 Peptide . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 40
2.23 ATP . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 42
2.24 Collagen . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 42
2.25 ATP . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 43
3.1 Difference between a catalysed & uncatalysed reaction . . . . . . . . . . . . . 46

3.2 lockandkey . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 47
3.3 inducedfit . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 47
3.4 Measuring the rate of reaction, using catalase. . . . . . . . . . . . . . . . . . . 48
3.5 The effect of enzyme concentration on the rate of an enzyme-catalysed reaction. 48
3.6 The effect of substrate concentration on the rate of an enzyme-catalysed reaction. 49
3.7 The effect of temperature on an enzyme-catalysed reaction . . . . . . . . . . . 50
3.8 The effect of pH on an enzyme-catalysed reaction . . . . . . . . . . . . . . . . 51
3.9 Competitive and non-competitive inhibitors – the principles . . . . . . . . . . 52
4.1 ATP . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 56
4.2 ATP . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 57
4.3 Role of ATP synthase in the formation & breakdown of ATP . . . . . . . . . . 57
4.4 Mitchell’s chemiosmotic theory . . . . . . . . . . . . . . . . . . . . . . . . . . 58
032
4.5 Chloroplast . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 58
4.6 Chloroplast . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 59
4.7 Chlorophyll molecule . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 59
4.8 Light harvesting centre . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 60
214
4.9 Chlorophyll absorbs blue & red light the most, other wavelengths are absorbed
less . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 60
4.10 Photosynthetic action spectrum . . . . . . . . . . . . . . . . . . . . . . . . . . 61
4.11 Limiting factors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 67
733
5.1 The mitochondrion . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 69
5.2 For each molecule of glucose: . . . . . . . . . . . . . . . . . . . . . . . . . . . . 70
5.3 The link reaction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 71
o0
5.4 The Kreb cycle . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 72

5.5 Electron transport chain . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 73
5.6 Anaerobic respiration . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 75
oy
6.1 Development of pollen grain . . . . . . . . . . . . . . . . . . . . . . . . . . . . 78

6.2 Structure of ovule . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 79
F. M
6.3 Development of ovule . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 79

6.4 Double fertilisation . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 80
7.1 A comparison of blood vessels . . . . . . . . . . . . . . . . . . . . . . . . . . . 84

7.2 Structure of a vein . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 85
7.3 Vein under a microscope . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 85
Mr
7.4 Structure of haemoglobin . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 86

7.5 Oxygen dissociation curve for a foetus . . . . . . . . . . . . . . . . . . . . . . . 87
7.6 Carbon dioxide transport in the blood . . . . . . . . . . . . . . . . . . . . . . . 88
7.7 Oxygen dissociation curve for humans . . . . . . . . . . . . . . . . . . . . . . 89
7.9 Pressure changes during the cardiac cycle . . . . . . . . . . . . . . . . . . . . . 91
7.10 Atrial diastole . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 91
7.11 Atrial systole . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 92
7.12 Ventricular systole . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 93
7.13 Ventricular diastole . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 94
7.15 Myogenic stimulation . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 95
7.16 Oxygen dissociation curve for myoglobin . . . . . . . . . . . . . . . . . . . . . 97
8.1 The cell cycle . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 100
8.2 The cell cycle . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 101
8.3 Interphase . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 101
8.4 Prophase . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 102
8.5 Metaphase . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 102
8.6 Anaphase . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 103
8.7 Telophase . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 103
8.8 Cytokinesis in animal cells . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 104
8.9 Cytokinesis in plant cells . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 105
8.10 Overview of meiosis . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 109
8.11 Prophase I . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 110
032
8.12 Metaphase I . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 111
8.13 Anaphase I . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 111
8.14 Telophase I . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 111
8.15 Prophase II . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 112
214
8.16 Metaphase II . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 112
8.17 Anaphase II . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 112
8.18 Telophase II . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 112
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8.19 Crossing over . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 113
8.20 . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 115
8.21 . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 115
o0
9.1 Pentose sugar . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 118

9.3 Nucleotide . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 118
9.4 Nucleotide . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 118
9.5 Dinucleotide . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 119
oy
9.6 Dinucleotide . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 119

9.7 Base pairing . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 120
F. M
9.8 Structure of DNA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 120

9.9 Structure of DNA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 121
9.10 Structure of tRNA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 122
9.11 The process of DNA replication. . . . . . . . . . . . . . . . . . . . . . . . . . . 123
9.12 Three different theories of DNA replication . . . . . . . . . . . . . . . . . . . . 124
9.13 DNA polymerase only travels in the 3’ to 5’ direction only . . . . . . . . . . . 125
Mr
9.14 DNA replication . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 126

9.16 Transcription . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 127
9.17 Transcription . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 128
9.15 A summary of the experiment carried out by Meselson and Stahl . . . . . . . 129
9.18 Summary of translation . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 131
10.1 Different allele combinations . . . . . . . . . . . . . . . . . . . . . . . . . . . . 136

10.2 Full genetic cross . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 138
10.3 Cross between F1 pea plants using a punnet square . . . . . . . . . . . . . . . 139
10.4 Incomplete dominance in snapdragon plants. (a) Crossing two pink-flowered
snapdragon plants & (b) crossing a pink-flowered snapdragon with a white-
flowered snapdragon. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 140
10.5 Inheritance of sex-linked traits . . . . . . . . . . . . . . . . . . . . . . . . . . . 141
10.6 Inheritance of sex-linked traits . . . . . . . . . . . . . . . . . . . . . . . . . . . 142
10.7 Dihybrid inheritance . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 145
10.8 Dihybrid inheritance . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 146
11.1 Stabilising selection . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 156

11.2 Stabilising selection in birth mass in human babies. The red line represents
mortality rate. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 156
032
11.3 Directional selection . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 156
11.4 Disruptive selection . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 157
214
List of Tables
1.1 Differences between light & electron microscope . . . . . . . . . . . . . . . . . 5

733
1.2 Structure & function of different organelles . . . . . . . . . . . . . . . . . . . . 8
1.3 Differences between prokaryotes & eukaryotes . . . . . . . . . . . . . . . . . . 20
5.1 Complete breakdown of glucose . . . . . . . . . . . . . . . . . . . . . . . . . . 73

o0
5.2 ATP used & generated . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 74

5.3 energy values . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 75
oy
8.1 Differences between mitosis in plants & animals cells. . . . . . . . . . . . . . . 105

8.2 Differences between mitosis & meiosis . . . . . . . . . . . . . . . . . . . . . . . 114
F. M
9.1 Differences between DNA and RNA . . . . . . . . . . . . . . . . . . . . . . . . 122

9.2 Comparison between replication & transcription . . . . . . . . . . . . . . . . . 130
10.1 Incomplete dominance inheritance . . . . . . . . . . . . . . . . . . . . . . . . . 139

Mr
2
032
0 3
214
Lower Six
1 4
2
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3 3
7
o0
o 0
oy
oy
F. M
. M
F
Mr
r
M
Mr
F. M
oy
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733
214
032
1 Cell Structure and Function
032
1.1 Objectives
214 1.1 Objectives . . . . . . . 3
733
Objectives 1.2 Microscopy . . . . . . 3
1.2.1 Microscope . . . optical
§ Microscopy
microscope . . . . . . . 3
∗ calibrate eyepiece graticule
1.3 Plant and Animal
∗
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draw and determine linear dimensions of specimens

Cells . . . . . . . . . . 6
∗ distinguish between magnification and resolution
1.3.1 Plant cells . . . . . . . . 6
∗ prepare temporary slides
1.3.2 Animal cells . . . . . . . 6
§ Animal and plant cells
oy
1.4 Organelles & func-

∗ identify plant and animal cells tions . . . . . . . . . . 7
∗ compare plant and animal cells 1.4.1 Nucleus . . . . . . . . . 9
1.4.2 Cytoplasm . . . . . . . . 10
F. M
§ Organelles and their functions 1.4.3 Endoplasmic reticulum 10

∗ outline the functions of organelles 1.4.4 Rough endoplasmic
reticulum . . . . . . . . 10
§ Eukaryotic and Prokaryotic Cells 1.4.5 Smooth endoplasmic
∗ compare eukaryotic and prokaryotic cells reticulum . . . . . . . . 11
1.4.6 Ribosomes . . . . . . . . 11
§ Movement of substances into and out of cells
Mr
1.4.7 Golgi apparatus . . . . 12

∗ describe and explain the cell surface membrane structure 1.4.8 Mitochondrion . . . . . 12
∗ relate the structure of the membrane to movement of substances 1.4.9 Chloroplast . . . . . . . 13
into and out of cells 1.4.10 Centriole . . . . . . . . . 13
1.4.11 Cell membrane . . . . . 13
1.5 Eukaryotic & Prokary-
otic cells . . . . . . . . 18
1.2 Microscopy 1.5.1 Prokaryotic cells . . . . 18
1.6 Movement of sub-
stances into and out of
1.2.1 Microscope . . . optical microscope cells . . . . . . . . . . . 20
1.6.1 Transport across
§ optical microscope uses a mirror & condenser lens to illumi- membranes . . . . . . . 20
nate a specimen by projecting light onto it 1.6.2 Diffusion . . . . . . . . . 21
1.6.3 Active transport . . . . 22
§ the image is focused & magnified by objective & eyepiece
1.6.4 Osmosis . . . . . . . . . 22
lenses 1.6.5 Endocytosis & exocyto-
sis . . . . . . . . . . . . . 23
1.7 Questions . . . . . . . 24
4 CHAPTER 1. CELL STRUCTURE AND FUNCTION
Figure 1.1: Optical microscope
§ the total magnification is calculated by multiplying the num-

ber on the eyepiece & the number on the objective lens
§ creating an enlarged image does not necessarily provide the
observer with more information
• to achieve that, the image not only has to be enlarged but must also
show detail (resolution)
§ magnification is the number of times a specimen is enlarged

§ resolution is the ability to distinguish between two points
that are close together as separate entities
Electron microscope
§ the specimen is illuminated by an electron beam
§ the electron beam is focused using electromagnets arranged
around the path of the electron beam
§ electrons produce an image when focused onto a fluorescent
screen
1.2. MICROSCOPY 5
§ they can produce images with a magnification of up to x 500

000
§ a vacuum is required since electrons can be scattered by air
particles
§ electron beams have wavelengths much shorter than the
wavelengths of visible light.
• the resolving power is inversely proportional to the wavelength of
the radiation it uses
• an electron microscope therefore has a much greater resolving
power
§ there are two types (TEMs) & (SEMs).
032
§ electrons pass through a thin section of the specimen in a
TEM
§ in SEMs the electrons are reflected off the prepared surface
of the specimen
214
§ SEMs are very useful for detailed study of surfaces.
Differences between light & electron microscope

733
Feature Light microscope Electron microscope
radiation light rays beam of electrons
radiation source sun or light bulb electron gun
nature of lenses glass to focus light rays electromagnets which focus elec-
o0
tron beams
lenses used condensor, objective & eye piece condensor, objective & eyepiece
lenses lenses
image seen directly by eye a fluoresent (TV) screen is re-
oy
quired
magnification up to x 1,500 up to x 500,000
limit of resolution 200 nm 0.2 nm
stains dyes heavy metals
F. M
what it can show structure & arrangement of tis- can only show dead structures.
sues, microscopic organisms, liv- shows cell ultrastructure includ-
ing or dead, but it cannot show ing the fine structure of cell or-
the cell ultrastructure ganelles.
Mr
Magnification
𝐼𝑚𝑎 𝑔𝑒 ´ 𝑠𝑖𝑧𝑒
𝑀 𝑎 𝑔𝑛𝑖 𝑓 𝑖𝑐𝑎𝑡𝑖𝑜𝑛 “
𝐴𝑐𝑡𝑢𝑎𝑙 ´ 𝑠𝑖𝑧𝑒
𝐼𝑚𝑎 𝑔𝑒 ´ 𝑠𝑖𝑧𝑒
𝐴𝑐𝑡𝑢𝑎𝑙𝑠𝑖𝑧𝑒 “
𝑀 𝑎 𝑔𝑛𝑖 𝑓 𝑖𝑐𝑎𝑡𝑖𝑜𝑛
§ Image size observed size of the image (that is, what you can
measure with a ruler)
§ Actual size is actual size (that is, the real size – for example,
the size of a cell before it is magnified)
• 1cm = 10´ 2 m
• 1mm = 10´ 3 m
• 1𝜇m = 10´ 6 m
• 1nm = 10´ 9 m
1.3 Plant and Animal Cells
032
1.3.1 Plant cells
214
733
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oy
F. M
1.3.2 Animal cells

Mr
1.4. ORGANELLES & FUNCTIONS 7
1.4 Organelles & functions
§ cell membrane
• it has a trilaminar appearance
• it consists of mainly lipid & protein
• it controls exchange between the cell & its environment
§ cytoplasm
• it refers to all the living parts of the cells, excluding the
nucleus
• it consists of membrane-bound organelles & the cytosol
032
(the fluid part of the cytoplasm)
§ cytoskeleton
• consists of microtubules, filaments & fibres
• it gives the cytoplasm physical support
214
• it is also involved in cell movement 733
o0
oy
F. M
Mr
Diagram Structure Function

Endoplasmic reticulum
§ a system of flattened membrane- § RER
bound sacs (cisternae )
• it has rib
§ it is continuous with the outer mem-
• transpo
brane of the nuclear envelope
ribosom
§ two types RER & SEM
nae, to t
§ SER
• has no r
• site of li
sis
• in the
032
zymes
many ch
Ribosome
214
§ made of proteins & RNA § protein synthe
§ they are about 25nm in diameter § they may form
§ consists of large & small subunit bosomes attac
§ smaller ribosomes are found in mi-
733
tochondria & chloroplasts
§ they can be on ER or free lying
Nucleus
§ enclosed by an envelope which has § it contains DN
o0
nuclear pores § genes control

§ it contains chromatin § the nucleolus
somes
• euchromatin stains lightly &
oy
has active DNA

• heterochromatin stains
deeply & has inactive DNA
F. M
§ it contains a nucleolus
Mitochondrion
§ range from 1-10 𝜇m long & 1𝜇m wide § involved in ge
§ enclosed by an envelope bic respiration
Mr
§ the inner membrane is folded to § cristae

form cristae
• site of o
• surface has stalked particles tion
§ it contains a matrix § matrix

• it contains circular , ribosomes • site of K
& phosphate granules
Cell surface membrane

§ Made of phospholipids and proteins § Controls the p
§ Surrounds the cell into and out o
Nucleolus
§ A dark, granular area inside the nu- § Synthesises rib
cleus that contains DNA and pro-
teins
Diagram Structure Function

Golgi apparatus
§ a stack of cisternae § it is a processing & packaging
structure
• it is continuously being
formed at one end & buds off
§ producing glycoproteins re-
quired in secretions
as vesicles at the other
§ producing secretory enzymes
§ secreting carbohydrates
§ transporting & storing lipids
§ forming lysosomes
Chloroplast
§ it is about 5-10 𝜇m long § it is the site of photosynthesis
032
§ it is surrounded by an envelope § light energy is converted to
§ it contains a gel-like stroma chemical energy
§ the stroma has a system of mem-
branes called lamella
214
• the membranes contain
chlorophyll
• lamella are stacked to form
grana
733
Cell wall (in plants,algae
and fungi) § In plants, the cell wall is made of § The cell wall surrounds the cell
cellulose fibres and surrounds the membrane and stops the cell
o0
cell surface membrane bursting when it takes in water

§ Algal cell walls are typically made of by osmosis
glycoproteins and polysaccharides,
oy
§ fungal cell walls are usually made

of the carbohydrate chitin
F. M
1.4.1 Nucleus
§ enclosed by an envelope, composed of two membranes

§ it is perforated by nuclear pores
Mr
§ it contains chromatin (the hereditary material)

§ it contains a nucleolus
§ it is typically 10 𝜇𝑚 - 20 𝜇 m in diameter
§ it contains DNA
§ it controls cell’s activities
• through the manufacture of mRNA & tRNA

• hence it controls protein synthesis
§ the outer membrane is continuos with the ER

§ it may be covered with ribosomes
§ (ribosomes) which carry out protein synthesis
§ nuclear pores allow exchange of substances between the
nucleus & cytoplasm
Figure 1.2: Nucleus

§ nuclear pores control entry and exit of substances into the

nucleus
Nucleolus
§ found in the nucleus

§ it makes rRNA and assembles the ribosomes
§ the central core has DNA
§ around the central core is RNA
032
1.4.2 Cytoplasm
§ it is aqueous in nature with about 90 % water

§ it contains cell organelles
214
§ it contains insoluble water molecules
§ it contains insoluble storage molecules it has ions, sugar,
salts, amino acids, fatty acids, nucleotides, dissolved gases
733
in solution
§ there are proteins in colloidal solution
§ it stores vital chemicals
§ it is the site of metabolic pathways
o0
1.4.3 Endoplasmic reticulum

oy
§ a system of membranes in the cytoplasm

§ cannot be seen with a light microscope
F. M
§ it is sheet-like in nature
§ it is also tubular in nature
§ they are membrane bound sacs called cisternae
§ it has a single membrane
§ it is continuos with the outer membrane of the nuclear
envelope
Mr
1.4.4 Rough endoplasmic reticulum
§ it has ribosomes embedded on its surface

§ it transports proteins through the cisternae
§ proteins will be made by ribosomes on the ER surface
§ there are receptors on the ER membrane
032
Figure 1.3: Rough endoplasmic retic-
ulum
§ these receptors provide a channel through which proteins
214
can pass into the cisternae after synthesis
§ the protein is then transported through the cisternae
§ it is transported to the Golgi Apparatus
733
§ the protein is also modified in the cisternae
§ it can be modified into a glycoprotein
o0
1.4.5 Smooth endoplasmic reticulum
§ it has no ribosome embedded on its surface

oy
§ it is for steroid synthesis, a type of lipid

§ it is for lipid synthesis, storage and transport
§ it then passes them to the Golgi Apparatus
F. M
§ it synthesises, stores and transports carbohydrates
1.4.6 Ribosomes
§ they are about 20nm - 25 nm in diameter

Mr
§ they are the site of protein synthesis

§ it consists of 2 subunits
§ a large subunit and a small subunit
§ they are the last to be sedimented during sedimentation
§ 70s are found in prokaryotes, chloroplasts, mitochondrion
§ 80s are found in eukaryotes
§ 80s are larger than 70s
§ they have roughly equal amounts of RNA (rRNA) & protein
§ small subunit has one rRNA & 21 protein molecules
§ large subunit has two rRNA & 34 protein molecules Figure 1.4: Ribosomes
§ there are free ribosomes & ER bound ribosomes
§ many ribosomes can attach to an mRNA molecule
§ to form polysomes or polyribosomes
§ it is not surrounded by a membrane
1.4.7 Golgi apparatus
§ found in all eukaryotic cells

§ it is a stack of flattened sacs
§ the sacs are bound by a membrane
§ the sacs are called cisternae
§ it is associated with Golgi vesicles
§ proteins & lipids produced by the ER are passed through
the G.A
032
§ there is a forming face on the outer side
§ new cisternae are being formed
§ they are formed by vesicles from the SER & it is convex in
214
shape
§ there is a maturing face on the inner side
§ cisternae break up into vesicles & it is concave in shape
§ the G.A transports materials contained within it
733
§ it modifies materials contained within e.g proteins to glyco-
proteins
§ it modifies and labels proteins
§ it is highly active in secretory cells
o0
§ it forms lysosomes, it produces secretory enzymes & is

involved in carbohydrate secretion
oy
1.4.8 Mitochondrion
F. M
§ it is rod shaped
§ length is 1,5-10 𝜇m; width 0.25 - 1 𝜇m; diameter less than 1
𝜇m
§ it is envelope bound
§ inner membrane is folded to from cisternae
Mr
§ inner membrane has stalked particles/ATP synthase

§ inner membrane has enzymes for ETC
§ inner membrane is the site of the ETC & oxidative phospho-
rylation
§ ATP synthase/stalked particle catalyses ATP production
from ADP + P𝑖
§ using energy from chemiosmosis of protons
§ it contains an inner matrix
Figure 1.5: Golgi apparatus
§ matrix has 70s ribosomes, circular DNA & P𝑖
§ matrix has enzymes for the Kreb’s cycle & it is the site of the
Kreb’s cycle
§ intermembrane space has a low pH
§ it is for the accumulation of 𝐻 ` used in the ETC
§ they are able too move & change shape
Figure 1.6: Mitochondrion

§ the outer membrane has a transport protein called porin
1.4.9 Chloroplast
§ 3 -10 𝜇m in diameter
§ it is surrounded by an envelope
§ it has a gel-like stroma
§ there are fluid filled sacs, called thylakoids
§ these are stacked to form grana
§ grana are linked /connected by middle lamellae
§ they contain chlorophyll & other photosynthetic pigments
032
§ these are located on a system of membranes
§ thylakoids contain enzymes for the light dependent photo-
synthesis
214
§ thylakoids ate the site of light dependent photosynthesis
§ stroma has enzymes, sugars, organic acids, starch
§ stroma is the site of light-independent stage
§ stroma contains DNA & ribosomes
733
§ so as to quickly manufacture some proteins needed for
photosynthesis
o0
1.4.10 Centriole Figure 1.7: Chloroplast
§ located in the cytoplasms near the nuclear envelope

oy
§ they are found in animals & some plants

§ they occur in pairs - two associated centrioles form a centro-
some
F. M
§ they are at right angles to each other

§ each is 500 nm long, 200nm in diameter
§ it has nine groups of microtubules
§ microtubules are arranged in triplets
§ neighbouring triplets are attached to each other by fibrils
Mr
§ each microtubule is 25nm in diameter

§ microtubules are hollow
§ microtubules are made of subunits of the protein tubulin
§ they are involved in orienting the spindle during nuclear
division
1.4.11 Cell membrane

Figure 1.8: Cetriole
Structure of cell membrane
§ it is approximately 7nm thick

§ has a basic structure of a phospholipid bilayer
§ it consists of phospholipids, proteins & cholesterol
032
Figure 1.9: Cell membrane 214
733
§ it consists of phospholipids in a bilayer arrangement
§ phospholipid tails point inwards, facing each other & forming
o0
a non-polar hydrophobic interior

§ phospholipid heads face the aqueous (water-containing)
medium that surrounds the membranes & inside of the cell
they act as barrier to most water soluble substances
oy
§
§ phospholipids move about by diffusion in their own layers
§ some of the phospholipid tails are saturated & some are
F. M
unsaturated
§ the more unsaturated they are, the more fluid the membrane
• because the unsaturated fatty acid tails are bent & therefore
fit together more loosely
§ proteins float about forming a fluid mosaic pattern

Mr
§ proteins have both regions of hydrophobic amino acids &

regions of hydrophilic amino acids
§ integral proteins are embedded through the membrane
§ peripheral proteins occur only on the surface
§ there are channel proteins with protein channels
§ there is cholesterol which increases flexibility & stability of
proteins
§ there are glycoproteins & glycolipids
§ carbohydrates may be attached to some of the proteins &
lipids on the outer surface, acting in part,
• as receptor sites,
• in cell-to-cell recognition or
• cell adhesion.
§ cholesterol has a hydrophilic head & hydrophobic tail, hence

they fit between phospholipid molecules
§ at low temperatures it increases membrane fluidity, prevent-
ing it from being too rigid
§ it stabilises the cell at higher temperatures preventing the
membrane from being too fluid
§ components can drift & change position (Fluid-Mosaic Model)
• ‘fluid’ because phospholipids & proteins can move
about by diffusion
• the phospholipids move sideways, mainly in their own
layers
032
• some proteins about within the phospholipid bilayer
• ‘mosaic’ describes the pattern produced by the scattered
protein molecules when the surface of the membrane is
viewed from above
Phospholipids
214
733
§ hydrophilic heads face outside the cell surface, attracted by
water on both sides
§ hydrophobic tails point towards the centre of the membrane,
o0
repelled by water
§ they allow lipid-soluble substances to enter or leave the cell
§ they prevent water-soluble substances entering or leaving
oy
the cell
§ they make the membrane flexible
§ they make the membrane self-sealing
F. M
Proteins
§ they are interspersed throughout the membrane

§ some occur in the surface of the bilayer (intrinsic proteins)
Mr
§ some can be in either layer some move between layers of the

bilayer (extrinsic)
§ they give mechanical support to the membrane
§ they (together with glycolipids) act as cell receptors
§ some proteins completely span the bilayer (intrinsic/inte-
gral/transmembrane)
§ they are channel proteins with protein channels, forming
water-filled tubes to allow water soluble ions to diffuse across
§ they are carrier protein
§ important in passive & active transport
§ they bind to ions or molecules like glucose & amino acids
§ then change shape in order to move these molecules across
the membrane
§ they help cells adhere together

§ they form cell-surface receptors for identifying cells
Cholesterol
§ they occur within the phospholipid bilayer

§ it adds strength to the membrane
§ they are hydrophobic
§ prevents loss of water and dissolved ions from the cell
§ they reduce lateral movement of other molecules including
phospholipids
032
§ they make the membrane less fluid at high temperatures
Glycolipids
214
§ its a carbohydrate covalently bonded with a lipid
§ the carbohydrate extends from the phospholipid bilayer into
the aqueous environment outside the cell
733
§ it acts as a cell-surface receptor for specific chemicals
§ they help maintain the stability of the membrane
§ help cells attach to one another and form tissues
o0
Glycoproteins
oy
§ carbohydrates which are attached to extrinsic proteins on

the outer surface of the cell membrane
F. M
§ they act as recognition sites

§ they act as cell-surface receptors for hormones & neurotrans-
mitters
§ help cells attach to one another & form tissues
§ allows cells to recognise one another
Mr
1.5. EUKARYOTIC & PROKARYOTIC CELLS 17
Cell membrane functions

Component Roles
Phospholipids Form the fluid bilayer that is the fundamental structure
of thee membrane. Prevent hydrophilic substances –
such as ions & some molecules – from passing through.
Cholesterol Helps to keep the cell membrane fluid
Proteins & glycoproteins Provide channels that allow hydrophilic substances
to pass through the membrane; these channels can be
opened or closed to control the substances’ movement.
Actively transport substances through the membrane
against their concentration gradient, using energy de-
rived from ATP. Act as receptor molecules for sub-
stances such as hormones, which bind with them. Cell
032
recognition – cells from a particular individual or a
particular tissue have their own set of proteins & glyco-
proteins on their outer surfaces.
Glycolipids Cell recognition & adhesion to neighbouring cells to
214
form tissues.
§ phospholipids
733
• provide the basic structure of membranes
• marks boundaries of cells
• provide separate intracellular compartments, thus isolating
different
o0
§ channel proteins & carrier proteins

• involved in selective transport of polar molecules & ions
oy
§ enzymes
• proteins act as enzymes e.g microvilli on epithelial lining of
F. M
intestines
§ receptor molecules
• for chemical signalling between cells
§ antigens
• they act as cell identity markers
Mr
• they are glycoproteins

• they enable cells to recognise other cells
§ glycolipids
• they act as receptor sites for chemical signals
§ energy transfer
• it is involved in photosynthesis & respiration
§ cholesterol
• it acts as a plug restricting movement of substances across the
membrane
032
214
1.5 Eukaryotic & Prokaryotic cells
733
Prokaryote Eukaryote
average diameter of cell is 0.5–5𝜇m cells commonly up to 40𝜇m diameter

no distinct nucleus distinct, envelope bound nucleus
no membrane bound organelles membrane bound organelles present
o0
no chromosomes - circular DNA chromosomes present with DNA

no membrane bound organelles membrane bound organelles present
no chloroplast - only photosynthetic lamel- chloroplast present in plants
lae
smaller ribosomes (70S) larger ribosomes (80S)
oy
flagella lacks 9+2 internal arrangement flagella has 9+2 internal arrangement
F. M
1.5.1 Prokaryotic cells
§ they are smaller than eukaryotic cells

§ they have no true nucleus/no nuclear envelope
§ 0.1-10 𝜇m
Mr
§ cellwall made of murein, a peptidogylcan

§ some have a capsule which is slimy
§ they have 70s ribosomes, which are smaller than 80s
§ they store food reserves as glycogen granules & oil droplets
§ they have circular DNA
§ they have extra smaller circular DNA called plasmid
§ plasmid can replicate independently
§ they (plasmid) confer extra characteristics e.g resistance to
antibiotics
Figure 1.11: Prokaryotic cells
§ Cell wall
• protects bacteria against certain substances
1.5. EUKARYOTIC & PROKARYOTIC CELLS 19
• protects against mechanical damage

• prevents osmotic
§ Capsule
• protects against other cells (e.g WBC)
• helps bacteria to stick together for further protection
• stops cell from drying out
• it stores toxins
§ Cell surface membrane
• acts as a differentially layer
• controls entry & exit of chemicals
032
§ Circular DNA
• has genetic information
• for replication of bacteria
214
• controls bacterial cellular activities
§ Plasmid
• possesses genes that may aid survival of bacteria
• e.g enzymes to breakdown antibiotics
733
o0
oy
F. M
Mr
Organelle Prokaryote Eukaryote

nucleus
§ no true nucleus § distinct nucleus
§ no nuclear envelope § nuclear envelope
DNA
§ not associated with proteins § associated with histone prote
§ extra DNA called plasmid § no plasmids
§ circular DNA § linear DNA
membrane
§ no membrane bound organelles § membrane bound organel
present
032
chloroplast
§ absent § present in plants & algae
§ chlorophyll associated with bacterial
membrane
214
ribosomes
§ 70s § 80s
§ smaller § larger
733
cellwall
§ murein (peptidoglycan) § cellulose or chitin
capsule
§ present § absent
o0
flagella
§ thinner § thicker
oy
§ no 9+2 arrangement § has 9+2 arrangement
reproduction
§ binary fission § asexual or sexual
F. M
cell type
§ multicellular § unicellular or multicellular
§ smaller § larger
Mr
1.6 Movement of substances into and out of cells
1.6.1 Transport across membranes
§ various terms are used to describe the movement of

substances between cells & into & out of a cell
§ they differ in the following respects
• the movement of substances may occur across a selectively
permeable membrane (such as the plasma membrane). A
selectively permeable membrane allows only specific
substances to pass.
1.6. MOVEMENT OF SUBSTANCES INTO AND OUT OF CELLS 21
• the substance whose movement is being described may be

water (the solvent ) or it may be the substance dissolved in
the water (the solute ).
• movement of substances may occur from higher to lower
concentrations (down the concentration gradient) or the reverse
(up or against the gradient).
• solute concentrations between two areas may be compared.
A solute may be hypertonic (a higher concentration of
solutes), hypotonic (a lower concentration of solutes), or
isotonic (an equal concentration of solutes) relative to
another region.
• the movement of substances may be passive or active. Active
032
movement requires the expenditure of energy & usually
occurs up a gradient.
214
1.6.2 Diffusion
§ net movement of substances from a region of higher

733
concentration to an area of lower concentration, without
energy expenditure.
§ this movement occurs as a result of the random & constant
motion characteristic of all molecules (atoms or ions),
o0
• motion that is independent from the motion of other molecules.
§ some molecules may be moving against the gradient &

oy
some molecules may be moving down the gradient

§ net is used to indicate the overall, eventual result of the
movement
F. M
§ after some time, a state of equilibrium is attained where

molecules are uniformly distributed but continue to move
randomly
§ it is affected by
1 steepness of the diffusion gradient
Mr
2 surface area through which diffusion occurs

3 distance over which it occurs
§ occurs when the membrane is permeable to the particles

§ non-polar small molecules diffuse freely
§ the hydrophobic interior of the membrane repels
positively/negatively charged particles
§ polar molecules such as water diffuse slowly,
§ small polar molecules easily pass compared to larger ones
Facilitated diffusion
§ facilitated diffusion is the diffusion of solutes or water

through channel proteins in the plasma membrane
§ channel proteins have a fixed shape

§ water can pass through the plasma membrane without the
aid of specialized proteins, but aquaporins increase the rate
of transfer by facilitated diffusion.
§ it does not require energy
§ facilitated diffusion can involve carrier proteins
§ these (carrier proteins) change shape when specific
molecules bind
§ movement is down a concentration gradient
§ it does not require energy
1.6.3 Active transport
§ it requires energy from the hydrolysis of ATP

§ movement of moleculesfrom a region of lower concentration
to a region of higher concentration
§ it uses carrier proteins
§ carrier proteins span the membrane and act as pumps
§ active transport is the movement of solutes against a
gradient & requires the expenditure of energy (usually ATP)
§ transport proteins in the plasma membrane transfer solutes
such as small ions (Na` , K` , Cl´ , H` ), amino acids, &
monosaccharides across the membrane.
1 the molecule/ion binds to receptors in the channel/carrier
protein on the outside of the cell
2 ATP binds on the carrier protein on the inside of the cell
• ATP is hydrolysed to ADP & P𝑖
3 binding of ATP causes the carrier protein to change shape

• opening to the inside of the cell
4 the molecule/ion is released to the inside of the cell

5 the P𝑖 is released and is free to recombine with ADP to form
ATP
Figure 1.12: Active transport 6 the carrier protein returns to its original shape
• the process is selective
1.6.4 Osmosis
§ osmosis is the diffusion of water molecules across a

selectively permeable membrane, from a region of higher
water potential to a region of lower water potential (from an
area containing less solute to an area containing more
solute), without the expenditure of energy
§ when water moves into a body by osmosis, hydrostatic
pressure (osmotic pressure) may build up inside the body
1.6. MOVEMENT OF SUBSTANCES INTO AND OUT OF CELLS 23
§ turgor pressure is the osmotic pressure that develops when

water enters the cells of plants & microorganisms.
§ plasmolysis is the movement of water out of a cell (osmosis)
that results in the collapse of the cell (especially plant cells
with central vacuoles).
§ in animal cells, an increase in hydrostatic pressure leads to
cytolysis
§ cytolysis, the cell cannot withstand pressure & the cell
membrane breaks & the cell breaks
§ it water leaves the cell it leads to crenation as the cell shrinks
§ plant cells gain water & become turgid
032
§ plant cells lose water & become plasmolysed
1.6.5 Endocytosis & exocytosis
214
Exocytosis
§ large molecules e.g enzymes, hormones & white cells cannot

733
move through channel/carrier proteins
§ exocytosis is when vesicles fuse with the plasma membrane
& release their contents to the outside of the cell.
• it is common when a cell produces substances for export
o0
§ vesicles are usually formed by the GA

oy
Endocytosis
F. M
§ endocytosis is the capture of a substance outside the cell

when the plasma membrane merges to engulf it
§ the substance subsequently enters the cytoplasm enclosed in
a vesicle
Mr
• phagocytosis (“cellular eating”) occurs when undissolved

material enters the cell. The plasma membrane wraps
around the solid material & engulfs it, forming a phagocytic
vesicle.white blood cells) attack & engulf bacteria in this
manner.
• pinocytosis (“cellular drinking”) occurs when dissolved
substances enter the cell. The plasma membrane folds
inward to form a channel allowing the liquid to enter.
Subsequently, the plasma membrane closes off the channel,
encircling the liquid inside a vesicle.
032
1.7 Questions
214
1) Active transport and facilitated diffusion are two ways by which substances cross plasma
(cell surface) membranes.
733
a) State one difference and one similarity between active transport and facilitated
diffusion. [2]
Vitamin C & D are essential for the correct functioning of the body. They are,
therefore taken into cells but take different routes across the plasma (cell surface)
o0
membrane. Vitamin C is water-soluble while Vitamin D is lipid-soluble.
b) Explain how the structure of the plasma (cell surface) membrane determines the
route taken by each of these vitamins. [4]
damage to cells. oy
Excessive concentration of salt in the blood and tissue fluid can cause serious
c) Explain the effects of a high concentration of salt on animal cells. [4]

F. M
2) The table below compares the features of a typical eukaryotic and prokaryotic cells.
Complete the table by placing one of the following, as appropriate, in each empty box in
the table:
a tick X
a cross ˆ
Mr
the words ”sometimes present“
eukaryotic cell prokaryotic cell

cell wall sometimes present X
nuclear envelope X
Golgi apparatus ˆ [6]
flagellum sometimes present
ribosomes X
carries out respiration X
chloroplast sometimes present
3) Substances cross the membranes of roots by a number of different methods, including
osmosis and active transport. Describe the processes of osmosis and active transport,
highlighting the differences between them. [7]
Table 1.3: Differences between

prokaryotes & eukaryotes
032
2 Biological Molecules and Water

214
733
2.1 Objectives
2.1 Objectives . . . . . . . 25
Objectives 2.2 Water . . . . . . . . . . 26
2.2.1 Biological significance 26
§ Carbohydrates
0
2.2.2 Functions of water . . . 28

∗ describe the formation and breakage of glycosidic bond
2.3 Carbohydrates . . . . 28
∗ describe the synthesis and molecular structure of polysaccharides
yo
2.3.1 Monosaccharides . . . . 28
∗ relate structures of polysaccharides to their functions in living
2.3.2 Disaccharides . . . . . . 29
organisms
2.3.3 Polysaccharides . . . . . 30
§ Lipids 2.3.4 Glycosidic bond . . . . 33
∗ identify lipids in different substances 2.4 Lipids . . . . . . . . . . 34
∗ describe the molecular structures of a triglyceride and a phospho- 2.4.1 Fatty acids . . . . . . . . 34
lipid 2.4.2 Triglycerides . . . . . . . 35
∗ relate the structures of triglycerides and phospholipids to their 2.4.3 Phospholipids . . . . . . 37
functions in living organisms 2.5 Proteins . . . . . . . . . 37
2.5.1 Amino acids . . . . . . . 37
§ Proteins
2.5.2 Bonds in Proteins . . . 38
∗ describe the structure of an amino acid 2.5.3 Structure of proteins . . 41
∗ outline the formation and breakage of a peptide bond
2.6 Questions . . . . . . . 44
∗ explain the meaning of the terms primary, secondary, tertiary
and quaternary structure’s of proteins
∗ describe the types of bonds which hold the protein molecules in
shape
∗ describe the molecular structures of haemoglobin and collagen
∗ relate the structures of haemoglobin and collagen to their func-
tions in living organisms
§ Water
∗ describe the structure & properties of water
∗ explain the roles of water in living organisms & as an environment
Common chemical § aldehyde

H C
groups
§ C
§ hydroxyl
§ C O
O
§ OH
§ keto C
26 CHAPTER 2. BIOLOGICAL MOLECULES AND WATER
§ carboxyl § keto
O § C O O´
§ C § O P O`
§ amino
OH H
§ carbonyl O
§ N
2.2 Water
§ made up of 1 oxygen, covalently bonded to 2 hydrogen

atoms
032
§ oxygen is more electronegative than hydrogen
• oxygen has a slight negative charge
• hydrogen has a slight positive charge
214
§ it is a polar molecule
§ its polarity leads to hydrogen bonding between
Figure 2.1: Water molecule different/separate water molecules
§ hydrogen bonds are individually weak but collectively
733
strong
o0
2.2.1 Biological significance
Solvent properties
oy
§ 1. Solvent properties
• it is a good solvent of polar substances
• molecules or ions of dissolved substance can move about
F. M
more freely
• this makes molecules and ions to be more chemically
reactive (as compared to their solid state)
• most cellular reactions occur in aqueous solutions
• it is important as a transport medium of dissolved
Mr
substances
• non-polar molecules (e.g lipids) are repelled by water
• such molecules group together in the presence of water
• this is important in;
∗ formation of cell membranes
∗ determining 3D structure of proteins & nucleic acids
High heat capacity
§ 2. High heat capacity

• it has a high specific capacity
• a lot of heat leads to a small temperature increase
2.2. WATER 27
• this is because a lot of energy is needed to break hydrogen

bonds
• this is important because
∗ temperature changes within water & water
environments are minimised
∗ biochemical reactions will will occur at more or less the
same temperature
∗ cells & organisms are provided with a very constant
environment
High heat of vaporisation
032
§ 3. High heat of vaporisation
• water has a high latent heat of vaporisation
• a lot of heat is needed to vaporise water
214
• water has a high boiling point
• to vaporise water, it takes a lot of energy from the
surroundings
• this assists in cooling animals during sweating & panting
733
High heat of fusion
o0
§ 4. High heat of fusion

• water has a high latent heat of fusion
• a lot of heat energy is needed to melt ice
oy
• a lot of heat must be lost to freeze water

• this means that cell contents are less likely to freeze
F. M
Maximum density at 4𝑂 C
§ 5. Maximum density at 4𝑂 C
• at less than 4𝑂 𝐶 the density of water decreases
• ice floats on liquid water
Mr
• this ensures that in cold climates, ice floats & insulates water
below
• this maintains circulation in water-bodies, which may result
in nutrient cycling
• animals are also protected from the cold
• it enables colonisation of new habitats
High surface tension & cohesion
§ 6. High surface tension & cohesion

• water has high tension & cohesive forces
• this is due to hydrogen bonds between water & other
substances
• high surface tension is important for small organisms which

enable them to settle on water
• water molecules can stick together & can be drawn up
through conducting tissues
• high cohesion is important in cells & translocation through
the phloem & xylem
Water as a reagent
§ 7. Water as a reagent
• water is a source of hydrogen during photosynthesis
• water is used during hydrolysis reactions
032
Water is incompressible
214
§ 8. Water is incompressible
• water cannot be compressed
• it is used for support in hydroskeletons
733
2.2.2 Functions of water
§ structural components of cells

o0
§ it is a solvent & a medium for diffusion & reactions

§ for support for aquatic organisms & as an hydroskeletons &
in plants
oy
§ it is used for swimming of gametes during fertilisation

§ used for dispersal of seeds
§ it is a reagent in hydrolysis & photosynthesis
F. M
§ transpiration
§ translocation of mineral salts & organic molecules
§ germination of seeds
§ transport of blood, lymphatic system & excretory systems
§ osmoregulation
Mr
§ cooling
§ protection e.g tears
2.3 Carbohydrates
2.3.1 Monosaccharides
§ single sugar units with the general formula 𝐶 𝑛 𝐻2 𝑛 𝑂 𝑛

§ trioses (3C), tetroses (4C), pentoses (5C), hexoses (6C),
heptoses (7C)
§ soluble in water
§ pentoses 𝐶5 𝐻10 𝑂 5 e.g ribose & ribulose
2.3. CARBOHYDRATES 29
032
214
733
Figure 2.3: Glucose isomers
o0
• used to make nucleic acids

• used to make coenzymes e.g NAD & NADP
• used to make ATP
•
oy
used to make RuBP

§ hexoses 𝐶6 𝐻12 𝑂 6 e.g glucose & galactose
• oxidised during respiration
F. M
• synthesis of disaccharides
• synthesis of polysaccharides
Glucose
Mr
§ exists as 𝛼 -glucose & 𝛽 -glucose isomers

§ in 𝛼 -glucose the -OH of carbon 1 is below the carbon
§ in 𝛽 -glucose the -OH of carbon 1 is above the carbon
2.3.2 Disaccharides
§ they are made up of 2 monosaccharides

§ joined together by a glycosidic bond
§ two monosaccharides react during a condensation reaction
to produce a disaccharide & water
§ numbers are used to indicate the carbon atoms involved in
the glycosidic bond
032
Figure 2.4: Disaccharides
214
• 1,4 glycosidic bond & 1,6-glycosidic bond
Maltose
733
• occurs as a breakdown product of starch by amylase
enzymes
• this occurs in the digestive system of animals &
germinating seeds
o0
• it is made up of 2 𝛼 -glucose units covalently joined

together
Figure 2.5: Maltose molecule
• it is a reducing sugar
oy
Lactose
F. M
• it is found in milk & is an energy source in milk

• it is made up of glucose & 𝛽 -galactose
• it is a reducing sugar
Sucrose
Mr
Figure 2.7: Sucrose molecule • it is commonly found in plants

• it is made up of 𝛼 -glucose & fructose
Figure 2.6: Lactose molecule • it is highly soluble & unreactive
• it is a transport carbohydrate in plants
• it is a non-reducing sugar
2.3.3 Polysaccharides
§ 3 - 10 monosaccharides units are oligosaccharides

§ 11 or more monosaccharide units are polysaccharides
§ normally each polysaccharide contains one type of
monomer
Figure 2.8: Starch-Amylose
§ they have no sweet taste & are insoluble in water

§ they are good storage compounds because
i they can form very compact molecules
• so large numbers can be stored/fit in a cell
032
ii glycosidic bonds are easily broken
• this allows rapid release of monosaccharides for respiration
iii they are not very soluble in water
214
• they have little effect on water potential within cells
Starch
733
§ it is a mixture of amylose & amylopectin
§ a polymer of 𝛼 - glucose
§ it is a storage carbohydrate in plants
o0
§ it is a major fuel in plants

§ it is easily converted to glucose:
• for respiration
oy
• to make cellulose in germinating seeds

• for other materials needed for growth
F. M
§ the starch molecule is stabilised by hydrogen binds between

different glucose residues
Amylose
Mr
§ has a straight chain structure

§ made of several thousand glucose residues
§ joined by 1,4 glycosidic bonds
§ glycosidic bonds cause the chain to coil helically into a
compact shape
!h
Amylopectin
§ it has a branched structure

§ it has thousands glucose residues joined by 1,4 & 1,6
glycosidic bonds
§ it has twice the number of glucose residues as amylose
Figure 2.9: Amylose
§ its chains are shorter than amylose
§ the branches are formed by 1,6 linkages
Figure 2.11: Amylopectin
032
Figure 2.10: Starch-Amylopectin
214
Glycogen
it is a storage carbohydrate in animals & fungi

733
§
§ it is made of 𝛼 -glucose
§ in vertebrates, it is found in the liver & muscles
§ its conversion into glucose involves hormones
o0
§ it has a branched structure

§ it has 1,4 & 1,6 glycosidic bonds
§ it has more branching compared to amylopectin
oy
§ it is larger than amylopectin

§ it forms many tiny granules which are usually associated
with the SER
F. M
Cellulose
§ a polymer of 𝛽 -glucose
§ about 10 000 glucose residues
Mr
§ it has a structural role
Figure 2.12: Cellulose

§ it is linked by 𝛽 -1,4 glycosidic bonds

§ successive glucose residues are linked at 180𝑂 to each other
§ it has straight chains
§ hydroxyl groups project outwards
§ forming hydrogen bonds with neighbouring chains
§ 60 -70 chains associate (due to hydrogen bonds) to form
microfibrils
§ microfibrils associate to form microfibrils
§ cellulose prevents cells from bursting
§ cellulose helps determine shapes of cells
032
214
733
o0

oy

F. M
2.3.4 Glycosidic bond
§ it is a bond between 2 monosaccharide residues

§ it is as a result of a condensation reaction
Mr
§ it can form between C1 & C4 or C1 & C6 of neighbouring

units
Figure 2.15: Condensation
Condensation
§ Condensation
• 2 -OH groups line next to each other
• one -OH combines with a hydrogen atom from another
-OH group
• to form a water molecules
• oxygen forms a bridge between adjacent
monosaccharide residues
• it is controlled by enzymes
§ Hydrolysis
• glycosidic bonds are digested in hydrolysis reactions
• a molecule of water is added as the glycolysis bond is
032
split
• it is a reversal of condensation
• it is catalysed by an enzyme
2.4 Lipids
214
733
§ water-insoluble organic substances which can be extracted
from cells by organic solvents
§ they are esters formed by a condensation reaction between
o0
fatty acids & alcohol

oy
2.4.1 Fatty acids
§ they contain the -COOH group (carboxyl group)

F. M
§ they have a general formula R.COOH

§ where R is H or a series of -CH2
§ most naturally occurring ones, have an even number of
carbons, between 14 & 22
§ hydrocarbon tails are hydrophobic/insoluble in water
§ the hydrocarbon tails cause lipids to be insoluble in water
Mr
§ some fatty acids are unsaturated/they contain double bonds

§ they form unsaturated lipids
§ polyunsaturated fatty acids have greater than 1 double
bonds
§ some fatty acids are saturated/ they have no double bonds
§ unsaturated fatty acids
Figure 2.16: Fatty acid • have lower melting points
• animal lipids are often unsaturated
§ saturated fatty acids
• have higher melting points
• plant lipids are often saturated
2.4. LIPIDS 35
2.4.2 Triglycerides Figure 2.17: Glycerol
§ most lipids are triglycerides

§ a glyceride is an ester formed by combining a fatty acid with
the alcohol glycerol
§ they are formed from glycerol (alcohol) & fatty acids
§ glycerol has 3 hydroxyl groups
§ each -OH is able to undergo a condensation reaction with a
fatty acid
§ triglycerides are non-polar
§ they have no uneven distribution of charge
032
§ they do not form hydrogen bonds with water
§ they are insoluble in water/they are hydrophilic
§ they are soluble in certain organic solvents (ethanol,
chloroform)
214
§ they are less dense than water
§ they float on top of water
§ the length of their hydrocarbon tails vary in length
733
o0
oy
F. M
Mr
032
214
733
o0
oy
F. M
Figure 2.18: Formation of triglyc-

erides
Mr
Functions
§ they act as energy stores (fats in animals & oils in plants)

§ they have a higher calorific value than carbohydrates
§ oxidation of a unit mass of lipids yields more energy than
oxidation of a unit mass of carbohydrates
§ because lipids have a higher proportion of hydrogen:oxygen
as compared to carbohydrates/ have more C-H bonds than
carbohydrates
§ it is stored around delicate organs such as kidneys
§ it acts as blubber in aquatic animals
§ it contributes to buoyancy
§ it is oxidised to produce metabolic water
§ which is important in animals habiting dry habitats
F. M 2.5. PROTEINS 37
Mr
Figure 2.19: Phospholipid
§ waterproofing .eg cuticle

§ myelin sheath
§ acts as an electrical insulator of the axon membrane
§ because it is a poor conductor of ions
§ so as to increase the speed of impulses
2.4.3 Phospholipids
§ they are lipids containing a phosphate group

§ one -OH in glycerol combines with phosphoric acid
§ to form a phosphate head
§ two -OH groups combine with fatty acids
§ to form phosphate tails
§ the phosphate head has an electric charge
§ it is soluble in water/ it is hydrophilic
§ it is polar
§ the tail is non-polar
§ it has no uneven distribution of charge
§ it is insoluble in water/ it is hydrophobic
§ polar heads face towards water/ interact with water
§ non-polar tails face away from water
Functions of phospholipids
2.5 Proteins
§ they are macromolecules

§ they made up of amino acids
§ they have the elements C, O, N & at times S
§ the sequence of amino acids is controlled by DNA
2.5.1 Amino acids
§ they are monomers for proteins

§ 20 are commonly found in proteins
§ plants can manufacture all the amino acids they need from
simpler substances
§ animals can not synthesise all the amino acids from simpler
source or from other sources
• these are called essential amino acids
§ animals use essential amino acids to manufacture other
amino acids
§ through a process called transamination
§ amino acids are amphoteric
• they can ionize to both acids & bases
§ they are zwitterions
• they have both positive & negative charges
Structure of amino acids
§ it has an alpha carbon

§ there is an acidic group, amine group, R group & H are
attached
§ the amine group is basic
`
– NH2 + H` â
ÝÝ
ÝÝ – NH3
á
§ the carboxylic group is acidic
– COOH â
ÝÝ
ÝÝ – COO´ + 𝐻 `
á
§ the R group is a variable side chain

• determines the uniqueness of each amino acid
2.5.2 Bonds in Proteins
Peptide bond
§ a reaction between two amino acids

032
2.5. PROTEINS 39
214
§ to form a dipeptide joined by a peptide bond
§ the amino group of one amino acid, react
§ with the carboxyl group of another amino group
§ in a condensation reaction, with the elimination of water
733
§ to form a covalent bond
§ called a peptide bond
§ a dipeptide has
o0
1 a free amino group at one end
2 a free carboxylic acid group
3 a peptide bond
oy
§ this enables the addition of many amino acids
§ many acids join to form a polypeptide
§ by a condensation reaction
F. M
Mr
Figure 2.20: Peptide bond
O
Ionic bond
R C
§ some R groups are acidic or basic
§ they exist in ionised form at certain pHs
O
§ acidic R groups have a negative charge Figure 2.21: Acidic group.
§ COOH dissociates & releases 𝐻 ` and remains with a
negative charge
§ basic R groups have a positive charge
§ NH2 has a high affinity for 𝐻 `
§ it accepts 𝐻 ` & becomes positively charged
§ positive/basic R groups from one amino acid
§ and negative/acidic R groups from another amino acid
§ are attracted to each other
§ forming ionic bonds
§ these are weaker than covalent bonds
§ in aqueous environments they can be broken by changing
pH
Figure 2.22: Peptide
Disulphide bond
SH § the R groups of cysteine contains -SH (sulphydryl)

§ when 2 cysteine molecules line up next to each other
H C H § neighbouring sulphydryl groups can be oxidised
H O § they then form a disulphide bond
§ the disulphide bonds can be in different;
N C C
• chains of amino acids e.g insulin
H OH • different parts of the same chain
H
§ in the same chain, they cause the chain to fold
§ into a particular shape
§ they are strong/ not easily broken
Hydrogen bond
§ H in 𝑁 𝐻2 or -OH group has a slightly positive charge

§ because the shared electrons in the group
§ are pulled more towards N or O atoms
§ the hydrogen is then attracted towards neighbouring O/N
§ which is more electronegative
§ e.g C=O and -NH groups
§ along the length of a polypeptide chain
§ they can form regular shapes e.g 𝛼 helix
§ individual H bond is weak
2.5. PROTEINS 41
§ their total effect is strong

§ because they occur frequently
Hydrophobic interactions
§ some R groups are non-polar & hydrophobic

§ e.g tyrosine & valine
§ in an aqueous environment
§ a polypeptide with many non-polar R groups
§ the chain folds so that the non-polar R groups, come into
close contact
032
§ and they exclude water
§ in globular proteins, they fold
§ to form roughly spherical structures
§ hydrophilic groups point outwards towards water
214
§ hydrophobic groups point inwards towards the centre
2.5.3 Structure of proteins

733
Primary structure
§ it is a sequence of amino acids in a polypeptide

o0
§ it is held by peptide bonds

§ it is controlled by the DNA sequence of bases
§ it dictates its biological function
oy
§ proteins differ in variety, order and number of amino acids

§ number of possible polypeptides (P) of length (L) with n
amino acids is given by
F. M
𝑃 “n 𝐿
Secondary structure
Mr
§ it is an addition to the primary structure

§ it is due to the regular or twisting of a polypeptide, or both
§ coiling produces an 𝛼 -helix
§ folding produces a 𝛽 -sheet
𝛼 helix
§ maintained by many H bonds
§ between neighbouring CO and NH groups
§ the H in NH is bonded to O in CO
§ of the 4𝑡 ℎ amino acid away
§ (amino acid 1 and amino acid 5 etc.)
§ it makes a complete turn every 36 amino acid
§ it is very stable
§ due to many H bonds
§ because because all CO and NH participate in H bonding
§ e.g keratin is completely 𝛼 helical
Figure 2.23: 𝛼 helix

Collagen
§ a structural protein
§ with a high tensile strength
§ 3 polypeptide chains are wound around each other
§ to form a triple helix
032
§ each chain has about 1000 amino acids
§ a complete collagen compound is called tropocollagen
§ each chain is in a loose helix form (not 𝛼 helix) the three
strands are held by H bonds
214
§ many triple helices lie parallel to each other
§ to form fibrils
§ triple helices have covalent bonds
§ between neighbouring chains
733
§ fibrils unite to form fibres
§ it is resistant to stretching
§ it is insoluble in water
it is a component of connective tissue, bones, tendons,
o0
§
cartilage
§ the secondary structure ifs the most most important
it is physically tough
oy
§
F. M
Mr
Figure 2.24: Collagen
𝛽 pleated sheet
§ it is made up of many adjacent chains
§ they are more extended than 𝛼 helices
2.5. PROTEINS 43
§ they are arranged parallel to each other

§ they can be running in the same directions
§ they can be running in opposite directions
§ they are joined by hydrogen bonds between C=O and NH
groups of one chain
§ there are also hydrogen bonds between C=O and NH of
adjacent groups
§ all C=O and NH are involved in hydrogen bonding
§ hence it is stable and rigid
Figure 2.25: 𝛽 sheet

Tertiary structure
§ it is due to the bending and folding of a polypeptide chain

§ it forms a precise, compact globular shape, unique to that
protein
§ it is maintained by the interaction of ionic,H,
disulphide,hydrophobic interactions
Quaternary structure
§ it consists of more than 1 polypeptide chain

§ separate chains are held together by hydrogen, ionic and
hydrophobic interactions
§ to form a complex biologically active molecule
§ there are non-polar (prosthetic) groups associated with the
protein
Haemoglobin
§ it has four separate polypeptide chains/globins

§ it has 2 alpha and 2 beta chains
§ each alpha chain has 141 amino acids
§ each beta chain has 146 amino acids
§ it has a hydrophilic side
§ the hydrophilic side is facing outward
§ towards the aqueous environment
§ this make it soluble in water
§ hydrophobic regions face inwards, away from water
§ it is folded to form a globular compact shape
032
214
733
o0
oy
F. M
2.6 Questions
Mr
1) a) i) State the components needed to synthesise a triglyceride. [2]

ii) Name the chemical reaction by which these components are joined. [1]
b) State one function of triglycerides in living organisms. [1]
Lipase is an enzyme that catalyses the hydrolysis of triglycerides. It is a soluble
globular protein. The function of an enzyme depends upon the precise nature of
its tertiary structure. The diagram below represents the structure of an enzyme.
The black strips represents the disulphide bonds which help stabilise its tertiary
structure.
c) i) Describe the nature of the disulphide bonds that help to stabilise the tertiary
structure of a protein such as lipase. [2]
ii) Name two other types of bonding that help to stabilise tertiary structure. [2]
Region A on the diagram is a secondary structure.
d) Describe the nature of region A. [2]

3 Enzymes
032
214
§ explain the mode of action of enzymes
§ follow the progress of an enzyme catalysed reaction 3.1 Properties of enzymes 46
733
§ explain factors affecting rate of enzyme catalysed reactions 3.2 Mechanisms of action/-
§ explain the effect of competitive and non – competitive Mode of action . . . . 46
3.2.1 Lock and key . . . . . . 46
inhibitors on enzyme activity
3.2.2 Induced fit . . . . . . . . 47
o0
3.3 Rate of enzyme activ-

§ they are biological catalysts ity . . . . . . . . . . . . 47
§ they speed up biological reactions but remain unchanged at 3.3.1 Factors affecting rate of
activity . . . . . . . . . . 47
oy
the end
3.3.2 Enzyme inhibitors . . . 51
§ they are protein in nature
3.4 Questions . . . . . . . 53
§ they are made by living cells
F. M
§ they act on substrates

§ they combine with substrates to form a temporary ES
complex
§ at the end of catalysis, the ES complex breaks down
§ to form the enzyme and products
Mr
E+Sâ
ÝÝ
ÝÝ ES â
á ÝÝ
ÝÝ EP â
á ÝÝ
ÝÝE+P
á
46 CHAPTER 3. ENZYMES
032
214
733
Figure 3.1: Difference between a
catalysed & uncatalysed reaction
o0
3.1 Properties of enzymes

oy
§ globular proteins
§ they are coded for by DNA
F. M
§ they are catalysts

§ their presence does not alter the nature of the products
§ they are specific/they catalyse only a specific reaction
§ the catalysed reaction is reversible
§ their activity is affected by pH, temp, substrate
concentration & enzyme concentration
Mr
§ they lower the activation energy of reactions they catalyse

§ they have active sites, where reactions occur
3.2 Mechanisms of action/Mode of action
3.2.1 Lock and key
§ enzyme (active site) has a specific shape

§ the shape is like a lock
§ a substrate fits perfectly into active site
§ like a key fitting into the lock
3.3. RATE OF ENZYME ACTIVITY 47
§ because the shape of the substrate

§ is complementary to that of the active site
§ the site on the enzyme where the substrate binds is the
active site
§ the substrate is held in place by temporary bonds
§ between the substrate and some R-groups of the enzymes
amino acids
§ to form an ES complex
§ after catalysis, products leave/escape from the active site
§ enzymes are very large compared to their substrates
§ active sites are usually small regions on the enzymes
032
§ the remaining part of the enzyme is important in
maintaining the globular shape of the enzyme
214
y 3.2.2 Induced fit
§ enzyme active sites are more flexible

§ the active site is modified
733
§ as the substrate interacts with the enzyme
§ the enzyme and substrate can change shape slightly
§ the amino acids of the active site
§ are moulded
o0
§ into a particular shape

§ which enables the enzyme to perform its catalytic function
oy
3.3 Rate of enzyme activity

F. M
§ it is a measure of the amount of substrate changed to

products
§ it is determined by measuring the slope of the tangent to the
curve
Figure 3.3: Induced fit
§ in the initial stage of the reaction
Mr
§ the steeper the slope, the higher the rate of reaction
3.3.1 Factors affecting rate of activity
§ enzyme activity is affected by:

• Enzyme concentration
• Substrate concentration
• Temperature
• pH
§ when investigating a factor;
i) all factors should be kept constant
ii) all factors should be at optimum levels
iii) initial levels only, should be measured
032
214
Figure 3.4: Measuring the rate of reaction, using catalase.
733
Enzyme concentration
§ the rate of reaction is proportional to enzyme concentration

§ increasing enzyme concentration, increases the rate of
o0
reaction
oy
F. M
Mr
Figure 3.5: The effect of enzyme con-

centration on the rate of an enzyme-
catalysed reaction.
Substrate concentration
§ increasing the substrate concentration causes the rate of

reaction to increase
§ V𝑚 𝑎 𝑥 occurs when increasing substrate substrate

concetration has no change in the rate of reaction
§ this is because all enzyme active sites will be saturated with
the substrate
§ any extra substrate has to wait until the ES complex has
released the products, before it enters
032
214
733
o0
oy
F. M
Figure 3.6: The effect of substrate concentration on the rate of an enzyme-catalysed reaction.
Temperature
Mr
§ at low temperatures, rate of reaction is low, because enzymes

are inactivated
§ increasing temperature, increases the Kinetic of enzymes &
substrates
§ increasing their chances of bumping together
§ increasing the probability of a reaction
§ the rate of reaction is doubled for every 10𝑂 𝐶 temperature
increase
§ up until the optimum temperature
§ this is the temperature that promotes maximum activity
§ increase in temperature beyond the optimum temperature,
decreases rate of reaction
§ because the enzyme is denatured
§ it has lost its secondary and tertiary structure

§ the precise structure of the active site is lost
§ hydrogen and hydrophilic interactions are broken
032
214
733
o0
oy
Figure 3.7: The effect of temperature

on an enzyme-catalysed reaction
F. M
pH
§ every enzyme functions most efficiently over a particular pH

range
§ usually it is a narrow pH range
Mr
§ maximum rate of reaction occurs at optimum pH

§ when pH is altered above or below optimum pH
§ rate of enzyme activity diminishes
§ at low pH, concentration of H` increases
§ this increases the number of positive charges
§ this alters the ionic charge of the acidic and basic groups
§ this disrupts the ionic bonding
§ which helps maintain the specific shape of the enzyme
§ pH change alters enzyme shape & active site
§ extreme pH denatures the enzyme
032
214
733
o0
oy
Figure 3.8: The effect of pH on an

F. M
enzyme-catalysed reaction
3.3.2 Enzyme inhibitors
§ these are substances which reduce the rate of enzyme

Mr
catalysed reactions
§ it can also regulate enzyme activity within cells
§ some drugs & poisons act as inhibitors
Competitive inhibitors
§ it has a structure similar to the substrate

§ it has a structure complementary to the active site
§ it fits into the active site of the enzyme
§ it does not take part on a reaction
§ it prevents the true substrate from entering the active site
§ it competes with the substrate for the active site
§ increasing the substrate concentration increases the rate of

reaction
Non-competitive inhibitors
§ they are structurally different from the substrate

§ their shape is not complementary to the active site
Figure 3.9: Competitive and non-competitive inhibitors – the principles
Non-competitive reversible
§ it combines with the enzyme away from the active site

§ it does not affect the ability of the substrate to bind with the
enzyme
§ it stops catalysis
§ rate of reaction decreases with increasing inhibitor
concentration
§ when inhibitor is saturated, rate of reaction will be almost nil
§ an increase in substrate concentration, does not affect the rate
of reaction
Non-competitive irreversible
§ they combine permanently with sulphydryl (-SH) groups

§ it may be in the active site or elsewhere
§ it changes the enzyme structure
§ it changes the enzyme active site
§ this reduces the rate of catalysis
3.4. QUESTIONS 53
§ this causes the protein of the enzyme to precipitate
Allosteric enzymes
§ these are enzymes which change shape

§ they are regulated by non-competitive inhibitors/allosteric
inhibitors
§ they bind to the enzyme at allosteric sites
§ these are specific sites away from the active site
§ they cause reversible change in the structure of the enzyme
§ they cause reversible change in the structure of the active site
032
3.4 Questions
214
733
o0
oy
F. M
Mr
032
214
733
1) Amylase is an enzyme which catalyses the hydrolysis of starch to maltose.
a) i) Name the bond which must be broken by this enzyme. [1]
o0
ii) Name the reagent that you would use to carry out a test for starch. [1]
iii) State the colour you would expect to see if you carried out the test before and
after the action of the enzyme. [2]
oy
In an investigation into the action of amylase, equal volumes of enzyme solution
and starch solution were mixed. The quantity of maltose produced was measured
during the course of two separate experiments, one carried out at 18 𝑂 𝐶 and the
F. M
other at 23𝑂 𝐶 . The results are shown in the diagram below.
Mr
b) i) Explain why the quantity of maltose produced eventually became constant. [1]
iii) Explain why, after 4 minutes, more maltose had been produced at 23𝑂 𝐶 than
at 18𝑂 𝐶 . [2]
The experiment was repeated with the same volume and concentration of amylase,
but with a higher concentration of starch solution.
c) Sketch on the diagram, the curve you would expect to obtain if the experiment
were repeated at 23𝑂 𝐶 with increased starch concentration. [2]
d) Explain the effects of reversible inhibitors on the rate of enzyme activity. [7]
4 ATP & Photosynthesis
4.1 Objectives
4.1 Objectives . . . . . . . 55
Objectives 4.2 ATP . . . . . . . . . . . 55
4.2.1 Uses of energy . . . . . 55
§ ATP Structure & Synthesis
4.2.2 ATP . . . . . . . . . . . . 56
• outline the need for energy in living organisms
4.3 Photosynthesis . . . . 58
• describe ATP structure as a phosphorylated nucleotide
4.3.1 Chloroplast . . . . . . . 58
• describe synthesis of ATP by chemiosmosis
4.3.2 Chlorophyll . . . . . . . 59
§ Photosynthesis 4.3.3 Absorption & action
• draw detailed structure of chloroplast spectra . . . . . . . . . . 60
• identify chloroplast pigments 4.3.4 Photosynthesis . . . . . 61
• discuss the role of chloroplast pigments in absorption & action spectra 4.3.5 Light-independent
• describe the photo-activation of chlorophyll reactions/Calvin cycle 64
• outline the Calvin Cycle 4.3.6 Limiting factors . . . . . 66
• discuss photosynthesis in C4 plants 4.4 Questions . . . . . . . 67
• discuss the concept of limiting factors
4.2 ATP
4.2.1 Uses of energy
§ synthesis of substances for growth & repair

§ active transport of substances in & out of cells
§ phagocytosis, pinocytosis & exocytosis
§ electrical transmission of nerve impulses
§ mechanical contraction of muscles & beating action of cilia &
flagella
§ heat energy released during respiration to maintain body
temperature
§ bioluminescence
56 CHAPTER 4. ATP & PHOTOSYNTHESIS
§ electrical discharge
4.2.2 ATP
032
214
733
Figure 4.1: ATP.
§ it is found in all organisms in exactly the same form

o0
§ hence it is a universal energy currency

§ it is a nucleotide made up of a base, pentose sugar and 3
phosphate groups
§ ATP is different from DNA bases
oy
• the base is always Adenine, instead of GTCA

• it has three phosphate groups instead of one
F. M
§ when a phosphate group is removed, ADP is formed & 30,5

kJ/mol of energy released
§ this reaction is reversible is catalysed by ATPase
ATPase
ATP + H2 O â
ÝÝ
ÝÝ
ÝÝÝ ADP ` H3 PO4 ` 30.5 kJ
Ýá
Mr
§ removal of second phosphate produces AMP & releases

30,5kJ/mol
§ removal of last phosphate leaves Adenosine & releases 14,2
kJ/mol
§ the phosphate bond in ATP is unstable, hence,
• ATP is not a good long-term energy store
• fats & carbohydrates are better long term energy stores
Properties of ATP
§ small - it moves easily in, out & within cells

4.2. ATP 57
§ water-soluble - most energy requiring processes occur in

water
§ contains bonds between phosphates with immediate
energy - large enough for cellular reactions, but not too large
that energy is wasted as heat
§ releases energy in small amounts - quantities useful for
energy reactions, so that energy is not wasted as heat Figure 4.2: ATP.
§ easily regenerated
Synthesis of ATP
032
§ it can be made using chemical potential energy (rearranging
chemical bonds)
§ it can also be made using electrical potential energy from the
transfer of electrons by electron carriers in mitochondria &
214
chloroplast
§ chemiosmosis involves the diffusion of electrons through a
partially permeable membrane in mitochondria &
733
chloroplasts
§ as protons diffuse, they release energy that is used to form
ATP from ADP & 𝑃𝑖
§ this process depends on the creation of a proton gradient
o0
§ the energy to do this comes from high energy electrons

• when pigment molecules are excited by absorbing light
• when high energy electrons are released when chemical
Figure 4.3: Role of ATP synthase in
oy
bonds are broken the formation & breakdown of ATP

F. M
Electron Transport Chain
§ it consists of a series of electron carriers, each with

progressively lower energy levels
§ as excited electrons move from carrier to carrier, energy is
released
Mr
§ this energy is used to pump protons across the membrane,

creating a proton gradient
§ proton the diffuse back through hydrophilic membrane
channels
§ the channels are linked to ATP synthase
§ the flow of protons through the channels, provides energy
used to build ATP from ADP and 𝑃𝑖
032
214
Figure 4.4: Mitchell’s chemiosmotic theory 733
4.3 Photosynthesis
4.3.1 Chloroplast
o0
oy
F. M
Mr
Figure 4.5: Chloroplast
§ approximately 3 𝜇m - 10 𝜇m long & 1𝜇m in diameter

§ it is surrounded by an envelope
§ they contain chlorophyll & other photosynthetic pigments
located in membranes
§ they have a ground substance/fluid-filled matrix called the
stroma
§ it contains starch grains, oil droplets & ribosomes
4.3. PHOTOSYNTHESIS 59
§ the membrane system is the site of light light-dependent

reactions
§ there are flattened fluid filled filled sacs called thylakoids,
Figure 4.6: Chloroplast
which form stacks called grana
§ stroma is the site of light-independent reactions
Adaptations of the chloroplast for light reactions
§ thylakoid membranes provide a large surface area for the

attachment of chlorophyll, for electron carriers & for
enzymes needed for light-dependent photosynthesis
032
§ a network of proteins in the grana hold the photosystems,
chlorophyll in a precise manner to allow maximum
absorption of light
§ granal membranes are selectively permeable which allows
214
for the establishment of a proton gradient
§ granal membranes have ATP synthase channels, which
catalyse the production of ATP
733
§ they have DNA & ribosomes so that they can quickly &
easily manufacture some of the proteins involved in
light-dependent reactions
o0
4.3.2 Chlorophyll
§ their function is to trap light energy, converting it to chemical

oy
energy
§ they are located in the thylakoids
F. M
§ they absorb red & blue-violet light & reflects green light
§ it has a head which has a Mg atom & a long hydrocarbon tail
• the tail projects into the thylakoid membrane & acts as
an anchor
§ chlorophyll a is the primary pigment

Mr
§ different pigments are embedded in the thylakoid membrane

to from a light harvesting system (LHC)
• these are chlorophyll b, xanthophylls & carotenoids
§ chlorophyll a is located in the reaction centre
§ the LHC & reaction centre form a photosystem (PS)
§ in PS I chlorophyll a is called P700,
§ in PS II chlorophyll a is P680
§ they differ slightly in their red absorption peaks
Figure 4.7: Chlorophyll molecule
Figure 4.8: Light harvesting centre
4.3.3 Absorption & action spectra
Figure 4.9: Chlorophyll absorbs blue

& red light the most, other wave-
lengths are absorbed less
§ absorption spectrum describes the different amounts of light

of different wavelength that a photosynthetic pigment
absorbs
§ absorption spectra for different pigments is obtained by
measuring their absorption of light of different wavelengths
§ an action spectrum is a graph showing the effectiveness of
different wavelengths of light in stimulating photosynthesis
§ an action spectrum demonstrates the rate of photosynthesis
according to the wavelength of light
§ the blue & red wavelengths give the highest rate of
photosynthesis
032
Figure 4.10: Photosynthetic action
spectrum
214
Excitation of chlorophyll
§ chlorophyll absorbs light & becomes excited

733
§ the energy from light boosts electrons to a higher energy
level
§ the light energy has been trapped & turned into chemical
energy
o0
§ the excited state is unstable & the molecules returns ot its

unexcited/ground state
§ as they return, their energy is lost by being passed from
oy
chlorophyll to an electron acceptor

§ the chlorophyll remains oxidised & the electron acceptor
F. M
becomes reduced
§ chlorophyll replaces its electron by getting it from an
electron donor
4.3.4 Photosynthesis
Mr
Light-dependent reactions
§ they occur in the thylakoid membranes

§ it breaks up H2 O in a photochemical reaction (photolysis) to
produce H`
2 H2 ÝÝÑ 4 H` + 4 e´ + O2
§ 𝐻 ` is used to reduce CO2

§ it produces ATP in photophosphorylation
• when ATP is made using light energy
§ when a chlorophyll molecule receives a photon of light;
• electrons are excited & raised to higher energy levels
• the electrons leave the chlorophyll molecule

• the electrons are collected by a carrier molecule (an
electron acceptor)
• the electrons enter the ETC & result in the synthesis of
ATP
Cyclic photophosphorylation
§ only involves PS I & drives the production of ATP only

§ when light hits a chlorophyll in PS I, an excited electron
leaves the molecule (photoactivation)
§ the electron is collected by an ETC to produce ATP
• as electrons fall back to their ground state
• their energy is used to pump H` from the stroma into
the thylakoid spaces
§ the electron then returns to PS I
§ NADPH + H` is not produced
Non-cyclic photophosphorylation
§ it involves PS I & PS II
§ there is photoactivation of electrons in both PS I & PS II
• both loose electrons & become unstable
§ electrons from PS II are lost & caught by electron acceptors &
transferred along an ETC to PS I
§ this drives the synthesis of one ATP molecule
§ (PS I receives an electron from the ETC & becomes stable)
§ electrons from PS I are excited & collected by an electron
acceptor
§ they are transferred along an ETC & collected by the
coenzyme NADP (Nicotinamide Adenine Dinucleotide
Phosphate)
§ NADP also collects H` to form NADPH + H`
§ reduced NAPD provides the hydrogen or reducing power in
the light-independent stage
Photolysis of H2 O
§ H2 O is split into H` , e & O2 using energy from the sun

§ the electrons released replace electrons from PS II
§ there is an enzyme in PS II which catalyses the breakdown of
H2 O
§ O2 is released as a by-product
§ protons are released into the thylakoid lumen
§ when protons return to the stroma, they combine with
NADP & an electron from PS I to form reduced NADP
(i) NADP is used in the light-independent stage
(ii) the process removes H from the stroma, hence helps
maintain the proton gradient
2 H2 ÝÝÑ 4 H` + 4 e´ + O2
Light-independent reactions
§ CO2 is converted into carbohydrates

§ it occurs in the stroma
§ it uses products of the light-dependent stage
Fixation
• CO2 combines with a 5C compound (RuBP) to form an

unstable 6C compound
• the reaction is catalysed by RuBP carboxylase-oxygenase
• the 6C compound quickly breaks down to form 2

molecules of a 3C glycerate -3 - phosphate
RuBISCO
RuBP + CO2 + H2 O ÝÝÝÝÝÑ 2 GP
Reduction
• GP is reduced using hydrogen from reduced NADP to

TP
• ATP from the light dependent stage is also used during
this process
• NADP is reformed & goes back to the light-dependent
stage
Regeneration
• 10 of every 12 TP molecules, the atoms are rearranged to

regenerate 6 molecules of RuBP
• the remaining 2 TP molecules of the 12 TP molecules are
the products of the Calvin cycle
• this process uses energy from ATP
§ 6 turns of the Calvin cycle are needed to form 2 molecules of
TP that can be used to make one glucose
4.3.5 Light-independent reactions/Calvin cycle

Uses of TP
32
§ used to synthesise organic compounds e.g sucrose, starch &
cellulose
140
§ some is used to synthesise amino acids, fatty acids & glycerol
§ the rest is used to regenerate RuBP
2
Adaptations for the light-independent stage
733
§ the stroma contains all the enzymes needed to carry out the
reactions
§ the stroma is membrane bound, creating & maintaining the
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ideal chemical environment with high concentrations of

enzymes & substrates
§ the stroma fluid surrounds the grana & so the products of
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the light-dependent reaction is the grana can readily diffuse

to the stroma
F. M
C4 photosynthesis
§ these are plants whose first product of photosynthesis is a 4C

acid in plants of tropical & subtropical climates,
• CO2 (not light) is the limiting factor of photosynthesis
Mr
• O2 from air becomes a competitive inhibitor of RuBISCO

• O2 combines with RuBISCO during photorespiration
• RuBP then breaks down to a 2C compound & TP,
reducing the yield of photosynthesis
§ the main photosynthetic cells (bundle sheath cells) are
surrounded by special mesophyll cells where C is fixed into a
4C compound (malate)
§ the 4C compound is moved into the bundle sheath cells
§ it breaks down to give CO2
• this ensures that the concentration of CO2 outcompetes
that of O2 at the active site of RuBISCO
§ acceptance of CO2 in mesophyll cells
• the CO2 acceptor PhosphoEnolPyruvate accepts CO2 to
form oxaloacetate
PEP + CO oxaloacetate
• the enzyme PEP carboxylase catalyses this reaction

• PEP carboxylase has a high CO2 affinity as compared to
RuBISCO
• PEP carboxylase is not inhibited by O2
§ oxaloacetate is converted to malate a 4C acid
NADPH + H` NADP`
oxaloacetate malate
§ malate shunt
• malate is shunted through the plasmodesmata to the
chloroplasts of the bundle sheath cells
• it is then converted to pyruvate & CO2
NADP` NADPH + H`
malate pyruvate + CO2
§ regeneration of CO2 acceptor

• pyruvate is returned to the mesophyll cells
• it is then used to regenerate PEP by the addition of P
from ATP
2ATP 2ADP
pyruvate phosphoenolpyruvate
4.3.6 Limiting factors
§ when one of the factors needed for photosynthesis is in short

supply, it reduces the rate of photosynthesis
§ it is therefore a reducing factor
§ light intensity
• light is needed as an energy source
• as light intensity increases, ATP & NADPH + H` are
produced at a higher rate
• increasing light intensity increases the rate of the light
dependent stage
• this will increase the quantity of ATP & NADPH + H`
• ATP & NADPH + H` are needed to convert GP into TP
• the concentration of TP will increase, which is needed to
regenerate RuBP
• very high light intensities may bleach chlorophyll &
slow down photosynthesis
§ CO2 concentration
• increasing the CO2 concentration increases the rate of
CO2 fixation in the Calvin cycle
• this increases the rate of photosynthesis, by increasing
the rate of TP production
§ T𝑂 C
• most stages are enzyme controlled & are T𝑂 C-sensitive
4.4. QUESTIONS 67
032
Figure 4.11: Limiting factors
214
4.4 Questions 733
1 a) By means of a large, fully labelled diagram, describe the structure of a chloroplast,
as disclosed by electron microscopy. [6]
b) Annotate your diagram to identify the function or role of the structures you labelled.
[4]
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c) In investigations of the physiology & biochemistry of photosynthesis, suspensions

of single-celled algae are often substituted for whole, green terrestrial plants.
Outline the advantages of this choice to the experimenter. [6]
oy
2 a) Show how both the absorption spectrum & the action spectrum of a particular
species of fresh water algae may be measured simultaneously.
b) Draw & fully label the absorption & action spectra you would expect to be produced,
F. M
using a single graph.

c) Describe in outline the steps by which the chlorophyll present in a sample of green
leaves can be obtained & the component pigments separated by means of paper
chromatography.
Mr
Mr
F. M
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214
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5 Respiration
5.1 Objectives
5.1 Objectives . . . . . . . 69
Objectives 5.2 Respiration . . . . . . 69
5.2.1 Mitochondrion . . . . . 69
§ draw detailed structure of mitochondrion
5.2.2 Glycolysis . . . . . . . . 70
§ outline the process of glycolysis 5.2.3 Link reaction . . . . . . 71
§ describe the formation of acetyl Coenzyme A (CoA) from 5.2.4 Krebs cycle . . . . . . . . 72
5.2.5 Electron Transport
pyruvate Chain . . . . . . . . . . . 73
§ outline the Krebs Cycle 5.2.6 Anaerobic respiration . 74
5.2.7 Energy values of differ-
§ explain decarboxylation and dehydrogenation in relation
ent substrates . . . . . . 75
to the link reaction and the Krebs cycle 5.2.8 Respiratory quotient . . 76
§ describe the process of oxidative phosphorylation in the 5.3 Questions . . . . . . . 76
mitochondrion
5.2 Respiration
5.2.1 Mitochondrion
§ 1 𝜇m in diameter & 3 - 10 𝜇m long

§ it is usually sausage shaped
§ it has an envelope with an intermembrane space
§ the inner membrane is folded to form finger-like cristae
§ its interior (the matrix) has an aqueous solution of
Figure 5.1: The mitochondrion.
metabolites & enzymes
§ there are 70s ribosomes & a small circular DNA
70 CHAPTER 5. RESPIRATION
5.2.2 Glycolysis
§ it does not need O2 & occurs in both aerobic & anaerobic

respiration
§ it occurs in the cytosol
§ glucose is converted 2 molecules of pyruvate
§ 2 phosphate groups, 2 molecules of NAD & 2 ATPs are
required
§ 4 ATPs & 2 NADH` 2 are produced
§ it is an example of substrate level phosphorylation
Figure 5.2: For each molecule of glucose:
1 phosphorylation of glucose
• this is done to make glucose more reactive
• 2 phosphate groups are added (phosphorylation) from 2
ATP molecules
• this provides the energy to activate glucose
• it lowers the activation energy for enzyme controlled
reactions
2ATP 2ADP
glucose fructose-1.6-bisphosphate
2 splitting of the fructose molecule

5.2. RESPIRATION 71
• each hexose is split into two 3C molecules called triose

phosphate
fructose-1.6-bisphosphate 2 triose phosphate
3 phosphorylation of triose phosphate

• an inorganic phosphate is added to each molecule of
triose phosphate
• to form trios-1.3-bisphosphate
P𝑖
triose phosphate triose -1.3- bisphosphate
4 oxidation of triose phosphate

• hydrogen is removed from each triose 1.3 bisphosphate
& transferred to NAD to form reduced NAD
`
NAD NADH2
triose -1.3 bisphosphate pyruvate
5 production of ATP
• each of the triose-1.3-bisphosphate molecules is
converted to pyruvate
• two ATP molecules are regenerated from 2 ADP
molecules
ADP 2ATP
triose -1.3 bisphosphate pyruvate
5.2.3 Link reaction
§ it occurs in the matrix of the mitochondrion

§ pyruvate diffuses through special channel proteins into the
matrix
§ CO2 is removed together with hydrogen to form an acetyl
group
§ hydrogen atoms are accepted by NAD
§ the acetyl group is bound by CoA to form acetyl CoA
Figure 5.3: The link reaction.

5.2.4 Krebs cycle
032
214
733
Figure 5.4: The Kreb cycle
§ the 2C acetyl group from acetyl CoA combines with 4C

oxaloacetate to form 6C citrate
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• CoA is released to be re-used again

§ citrate is dehydrogenated & decarboxylated to form a 5C
𝛼 -ketogluterate
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§ this releases a pair of hydrogen atoms which are accepted by

NAD (becoming reduced NAD), & one CO2
F. M
§ the 𝛼 -ketogluterate is dehydrogenated & decarboxylated to

form a 4C compound, a molecule of reduced NAD & a
molecule of CO2
§ the reorganisation of the four-carbon molecule provides
energy to phosphorylate ADP with a phosphate ion from the
Mr
matrix of mitochondria to form one ATP molecule directly

§ the next 4C compound is dehydrogenated, FAD acts is the
hydrogen & electron acceptor to become reduced FAD
§ a 4C molecule is dehydrogenated to reform oxaloacetate
§ the two hydrogen atoms are accepted by NAD to form
reduced NAD
§ the products of two turns of the Krebs cycle are
• six reduced NADs

• two reduced FADs
• four carbon dioxide molecules
• two ATP molecules produced directly
F. 5.2. RESPIRATION 73
Mr
5.2.5 Electron Transport Chain
§ it occurs in the cristae of the mitochondrion

§ the reduced NAD & FAD pass on their hydrogen atoms &
become oxidised so that can they can be used again
§ hydrogen atoms split into protons & electrons
§ electrons are passed from one carrier to another & their
energy is used to move protons from the matrix of the
mitochondrion into the intermembrane space
§ this creates a higher concentration of protons intermembrane
space than the matrix
• thereby setting a concentration gradient
§ protons pass back into the matrix through protein channels
§ 3 ATPS are made from NADH˚2 & 2 from FADH` 2
§ associated with each channel is the enzyme ATP synthase
§ an electron & proton are transferred to O2 forming H2 O
Figure 5.5: Electron transport chain
Table 5.1: Complete breakdown of

glucose
CO2 ATP NADH`
2 FADH`
2
glycolysis - 2 2 -
link reaction 2 - 2 -
Krebs cycle 4 2 +6 2
Total 6CO2 4ATP 10NADH`
2 2NADH`
2
§ Substrate level phosphorylation

• it occurs when a phosphate group and its associated
energy is transferred to ADP to form ATP
Table 5.2: ATP used & generated
ATP used ATP made difference
glycolysis -2 4 +2
link reaction 0 0 0
Krebs cycle 0 2 +2
ETC 0 34 34
Total -2 40 38
• the substrate molecule (the molecule with the phosphate
032
group) donates the high energy phosphate group
• such phosphorylation occurs during glycolysis.
§ Oxidative phosphorylation
• it occurs when a phosphate group is added to ADP to
214
form ATP
• the energy for the bond does not accompany the
phosphate group
• electrons in the electron transport chain of oxidative
733
phosphorylation supply the energy for the bond
• the energy is used to generate the H` gradient which, in
turn, supplies the energy to ATP synthases to generate
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ATP from ADP and a phosphate group

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5.2.6 Anaerobic respiration
§ for glycolysis to proceed, pyruvate & hydrogen must be

F. M
constantly be removed
§ it allows continued production of ATP even in the absence of
O2
§ in plants, bacteria & yeast pyruvate is converted to ethanol &
CO2
Mr
pyruvate + NADH`
2 ethanol + CO2 + NAD
§ pyruvate is decarboxylated to form ethanal & CO2

§ this reaction is catalysed by pyruvate decarboxylase
§ in animals pyruvate is converted to lactate
§ the reaction leading to ethanol cannot be reversed & the
remaining energy is wasted
§ in mammals, lactate is converted in the liver, back to pyruvate
pyruvate + NADH`
2 lactate + NAD
§ lactate dehydrogenase catalyses the reduction of pyruvate to

lactate & the oxidation of NAD.
5.2. RESPIRATION 75
Figure 5.6: Anaerobic respiration
5.2.7 Energy values of different substrates
Carbohydrates
§ glucose is the main respiratory substrate

§ brain cells & RBCs can only use glucose for respiration
§ starch & glycogen can be hydrolysed for respiration
§ disaccharides can be digested to monosaccharides for
respiration
§ monosaccharides (hexoses) can be changed by isomerase
enzymes to glucose for respiration
Lipids
§ lipids are first converted to fatty acids & glycerol

§ each fatty acid molecule is oxidised by the removal of 2C
acetyl fragments
§ the fatty acid molecule will be shortened 2C atoms at a time
§ each acetyl group is carried by CoA to form acetyl CoA
§ this can then enter the TCA cycle
§ the oxidation of lipids produces many hydrogen atoms,
which are used to from ATP during the ETC
§ hence lipids produce double the energy
Table 5.3: The energy values of dif-
ferent respiratory substrates.
Proteins
§ they are first hydrolysed to constituent amino acids

substrate mean energy
§ their amino groups are removed (deamination) value kJ/g
§ the remaining carbon skeletons enter the respiratory
pathway, depending on the number of carbon atoms they carbohydrates 15.8
have lipid 39.4
§ 3C compounds are converted to pyruvate protein 17.0
§ 4C & 5C compounds are fed into the TCA cycle
§ the greater the hydrogen atoms per molecule the more the
protons, the more the ATPs can be generated
032
5.2.8 Respiratory quotient
214
§ it is the ratio of CO2 produced by a respiring organism, to O2
consumed
733
𝑐𝑎𝑟𝑏𝑜𝑛 𝑑𝑖𝑜𝑥𝑖𝑑𝑒 𝑝𝑟𝑜𝑑𝑢𝑐𝑒 𝑑
𝑅𝑄 “
𝑜𝑥 𝑦 𝑔𝑒𝑛 𝑐𝑜𝑛𝑠𝑢𝑚𝑒 𝑑
o0
§ glucose
6
C6 H12 O6 + 6O2 ÝÝÑ 6CO2 + 6 H2 O 6 =1
oy
§ fatty acids
F. M
16
C15 H31 COOH + 23O2 ÝÝÑ 16CO2 + 16 H2 O 23 =
0.7
§ amino acids
4
Mr
CH3 COOH + 5O2 ÝÝÑ 4CO2 + 4 H2 O 5 = 0.8
§ if the RQ value is greater than the expected, it means there is

anaerobic respiration occurring
5.3 Questions
1) a) i) Name the nitrogenous base found in an ATP molecule. [1]

ii) Name the sugar found in an ATP molecules. [1]
b) ATP is described as having a universal role as the energy currency in all living
organisms. Explain why is described in this way. [4]
c) State precisely two places where ATP is synthesised in the cells. [2]
2) Succinate dehydrogenase is an enzyme located in the cristae of mitochondria. The
enzyme catalyses this reaction
succinate + FAD ÝÝÑ fumarate + reduced FAD
a) Describe the role of FAD in the reaction. [4]
b) The equation shows the complete oxidation of succinate.
C4 H4 O4 + 3 O2 ÝÝÑ 2 H2 O + 4 CO2
i) Calculate the respiratory quotient (RQ) for the complete oxidation of succinate.
[2]
ii) State the formula and show your working. [3]
6 Sexual Reproduction in plants
6.1 Objectives
6.1 Objectives . . . . . . . 77
Objectives 6.2 Sexual Reproduction in
Plants . . . . . . . . . . 77
§ Sexual Reproduction in Plants
6.3 Development of pollen
• describe anther structure & pollen formation
grains . . . . . . . . . . 78
• describe ovule development
• describe double fertilization 6.4 Structure of ovule . . 79
• explain the significance of double fertilisation in the embryo sac 6.4.1 Development of ovule . 79
6.5 Double fertilisation . 80
6.6 Questions . . . . . . . . 81
6.2 Sexual Reproduction in Plants
§ the production of offspring by the fusion of 2 gamete nuclei

to form a diploid zygote
§ at fertilization the nuclei of gametes fuse, bringing one set (n)
of chromosomes from each parent
§ to form 2 sets (2n) of chromosomes
§ gametes carry one set of chromosomes
• they are haploid
§ resulting offspring carry 2 sets of chromosomes
• they are diploid
§ during gametogenesis, meiosis occurs
• it reduces the diploid number of chromosomes to a
haploid number
• this ensures that during fertilisation, 2the diploid
number is restored
78 CHAPTER 6. SEXUAL REPRODUCTION IN PLANTS
6.3 Development of pollen grains
§ the anther has 4 pollen sacs (microsporangia)

§ pollen sacs produce pollen (microspores)
§ a diploid pollen mother cell (microsporocyte) undergoes
meiosis
§ to form haploid pollen grains (microspores)
§ after meiosis pollen grains are seen in groups of 4 called
tetrads
§ each grain develops a thick wall
• outer wall is called the exine, which is made of waterproof
032
sporopollenin
• inner wall is called intine
§ the pollen grain nucleus undergoes mitosis to form 2 nuclei
• generative nucleus
214
• pollen tube nucleus
microsporocyte ÝÝÑ tetrads ÝÝÑ microspore ÝÝÑ pollen grain, 2 nuclei

733
2n n n n
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F. M
Mr
Figure 6.1: Development of pollen

grain
6.4. STRUCTURE OF OVULE 79
6.4 Structure of ovule
§ one or more ovules develop

§ each ovule is attached to the ovary at the placenta
§ ovule is attached via/by the funicle
§ main body of the ovule is the nucellus
§ the nucellus is enclosed & protected by 2
sheaths/integuments
§ the integuments leave a small pore called the micropyle
032
214
733
Figure 6.2: Structure of ovule
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6.4.1 Development of ovule
§ inside the nucleus, nearest the micropyle one spore mother

cell developments
oy
§ this is the embryo sac mother cell

§ it undergoes meiosis to produce 4 haploid megaspore cells
F. M
§ one haploid cell furthest the micropyle develops to form the

embryo sac
§ embryo sac nucleus undergoes mitosis repeatedly to form 8
nuclei
§ four will be at each end of the embryo sac
only one is the female gamete
Mr
§
§ 2 nuclei (one from each polar end) migrate to the centre and
fuse to form a single 2n nucleus
§ 3 nuclei at each end develop their walls only one remains as
the gamete & other disintegrate
Figure 6.3: Development of ovule

80 CHAPTER 6. SEXUAL REPRODUCTION IN PLANTS
6.5 Double fertilisation
§ pollen grain lands on the stigma of compatible species, and it

germinates
§ stigma epidermal cells secrete a sucrose solution
§ the sucrose solution
1 stimulates germination of pollen grain
2 supplies food to the pollen grain
§ a pollen tube emerges from the pits & grows down the
hollow style to the ovary
§ growth is controlled by the tube nucleus
§ tube nucleus is found at the top of the growing tube
§ growth is due to
i auxins
ii positive chemotropism
iii negative aerotropism
§ as the tube grows, generative nucleus undergoes mitosis
§ to form 2 male gamete nuclei
§ pollen enters ovule through the micropyle
§ the tube nucleus degenerates & the tip bursts
§ the tip releases the male gamete nuclei
• one nucleus fuses with the the female gamete to form a 2n
zygote
• one fuses with 2n nucleus to form a 3n primary endosperm
nucleus
§ zygote becomes the embryo and primary endosperm
nucleus becomes the endosperm (food store)
§ double fertilization ensures that an endosperm is only
formed when a zygote/embryo is formed
§ this prevents unnecessary resource wastage
Figure 6.4: Double fertilisation

6.6. QUESTIONS 81
6.6 Questions
1)
032
214
733
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F. M
Mr
Mr
F. M
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214
032
7 Transport in animals
032
This chapter contains notes on transport in animals
214 7.1 Objectives . . . . . . . 83
733
7.2 Mammalian circula-
7.1 Objectives tory system . . . . . . . 83
7.3 Blood vessels . . . . . 84
Objectives 7.3.1 Arteries . . . . . . . . . . 84
o0
7.3.2 Veins . . . . . . . . . . . . 85
§ Mammalian circulatory system 7.3.3 Capillaries . . . . . . . . 85
• identify arteries, veins & capillaries 7.4 Oxygen transport . . . 85
• explain the role of haemoglobin in the transportation of oxygen & carbon 7.4.1 Structure of
oy
dioxide haemoglobin . . . . . . 85
• explain the Bohr effect 7.4.2 Structure of myoglobin
• explain the significance of the difference in the affinity for oxygen between: & foetal haemoglobin . 86
F. M
i. haemoglobin & myoglobin 7.4.3 Oxygen transport . . . . 87

ii. maternal & foetal haemoglobin 7.4.4 Carbon dioxide trans-
• describe the cardiac cycle port . . . . . . . . . . . . 88
• explain how heart action is initiated & controlled 7.4.5 Dissociation curve . . . 89
• explain the meaning of the terms systolic blood pressure, diastolic blood
7.5 Cardiac cycle . . . . . 91
pressure & hypertension
7.5.1 Myogenic stimulation
• discuss the long term consequences of exercise on the cardiovascular
Mr
of the heart . . . . . . . . 94
system
7.5.2 Regulation of heart rate 95
7.5.3 Exercise & cardiovascu-
lar system . . . . . . . . 96
7.6 Questions . . . . . . . 97
7.2 Mammalian circulatory system
§ very small organisms, can meet their requirements for the

supply of nutrients & oxygen, & the removal of waste
products, by means of diffusion
§ the very small distances that substances have to travel means
that the speed of supply or removal by diffusion is sufficient
for their needs
84 CHAPTER 7. TRANSPORT IN ANIMALS
§ these tiny organisms have a large surface area to total volume

ratio
§ so there is a relativity large area of membrane across which
gases can diffuse into & out of their bodies
§ larger, more active organisms cannot rely on diffusion alone
• cells deep within their bodies, are metabolically very active, with
requirements for rapid supplies of nutrients & oxygen, & with relatively large
amounts of waste products to be removed
• these organisms have well-organised transport systems, with pumps to keep
fluid moving through them
§ the blood (cardiovascular) system is made up of a pump, the

heart, & a system of interconnecting tubes, the blood vessels
032
7.3 Blood vessels
214
733
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Figure 7.1: A comparison of blood vessels

F. M
7.3.1 Arteries
§ they transport blood, swiftly & at high pressure, to the

tissues
§ they have a smaller lumen lumen relative to diameter
Mr
§ their walls are made up of three layers:

1 an inner endothelium (lining tissue), called the tunica intima, made up of a
layer of flat cells (squamous epithelium)
• this layer is very smooth, minimising friction with the moving
blood
2 a middle layer called the tunica media (‘middle coat’),
containing smooth muscle, collagen & elastic fibres
• it contains large amounts of elastic fibres
3 an outer layer called the tunica externa (‘outer coat’),
containing elastic fibres & collagen fibres
§ the elasticity of artery walls allows them to ‘stretch’, which
reduces the likelihood that they will burst
§ arteries branch out into smaller arterioles
7.4. OXYGEN TRANSPORT 85
§ blood has high pressure & moves in pulses

§ blood pressure drops significantly as blood flows through
the arteries
§ they have no valves except for the aorta & pulmonary artery
7.3.2 Veins
§ their walls have three layers, like arteries

§ they have thin muscular walls
§ they have little elastic tissue
§ they have a large lumen relative to diameter
032
§ they have valves along their length !h
§ blood flows from the capillaries into very small veins then
into larger veins
214
§ they return blood to the heart
• the inferior vena cava from the lower parts of the body
• the superior vena cava from the head & upper body
733
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Figure 7.2: Structure of a vein

F. M
Figure 7.3: Vein under a microscope
7.3.3 Capillaries
Mr
§ they have no muscle & no elastic tissue

§ they have a large lumen relative to diameter
§ they are permeable
§ they have no valves
§ they link arteries to vein
§ blood pressure in capillaries is reducing
7.4 Oxygen transport
7.4.1 Structure of haemoglobin
§ haemoglobin is the oxygen-carrying pigment in RBCs

§ it is a globular protein made of four polypeptide chains

• there are two identical alpha 𝛼 & two identical beta 𝛽
chains
§ each polypeptide chain contains an iron-containing haem
group
§ each haem group can bind with one oxygen molecule, so
each molecule of haemoglobin can carry 4 oxygen molecules
at a time.
§ the aggregation of several (4) polypeptide chains gives
haemoglobin a quaternary structure.
Figure 7.4: Structure of haemoglobin
7.4.2 Structure of myoglobin & foetal haemoglobin
§ myoglobin is a red pigment found in skeletal muscles with a

structure similar to haemoglobin
§ it has a higher affinity for oxygen compared to haemoglobin
§ foetal red blood cells are nucleated & contain foetal Hb
§ foetal Hb has two alpha ( 𝛼 ) & two gamma ( 𝛾 ) polypeptide
chains
§ it has a higher oxygen affinity compared to adult
haemoglobin
§ both myoglobin & foetal haemoglobin have higher oxygen
affinities so that they are able to take oxygen from adult
haemoglobin
§ the dissociation curves for both myoglobin & foetal Hb are
displaced to the left compared to adult Hb
§ myoglobin acts as an energy store for oxygen, only releasing
oxygen when supplies of oxyhaemoglobin are depleted
Figure 7.5: Oxygen dissociation

curve for a foetus
7.4.3 Oxygen transport
§ oxygen is transported by haemoglobin in RBCs

§ oxygen binds loosely to haemoglobin to form
oxyhaemoglobin
§ an iron atom (Fe II) is located within each haem group &
each of these can combine with one oxygen molecule
• the reaction is reversible
• Hb + 4 O2 â
ÝÝ
Ýá
Ý Hb(O2 )4
haemoglobin oxygen oxyhaemoglobin
§ oxygen binds to Hb under high oxygen partial pressures

(oxygen concentrations) such as in the lung alveolar
capillaries
§ oxygen is released from haemoglobin (Hb unloads) when
oxygen partial pressures are low e.g in capillaries of
respiring cells
• the release of oxygen is called dissociation
§ the addition of one oxygen molecule to the first haem group
distorts the shape of the haemoglobin molecule, making it
easier for the second oxygen molecule to combine with haem
§ this, in turn, makes it easier for the third oxygen molecule to
combine with a third haem group
§ it then becomes a little harder for the fourth oxygen molecule
to join the fourth haem group
§ this trend explains the sigmoid shape of the oxygen
dissociation curve.
7.4.4 Carbon dioxide transport
§ CO2 is transported in the blood in three different ways:

§ if CO2 accumulates in the blood it forms an acid solution &
could lead to fatal changes in blood pHs
032
Figure 7.6: Carbon dioxide transport
in the blood
214
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1. 85% as hydrogencarbonate ions, HCO´
3 , as described
above
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• H2 O + CO2 ÝÝ
âÝÝ H2 CO3 â
á ÝÝ
Ýá
Ý H+ + HCO3–
water carbon dioxide carbonic acid hydrogen ion hydrogen carbonate ion
oy
∗ one product of the dissociation of dissolved CO2 is

hydrogencarbonate ions, HCO˘3
F. M
∗ these are formed in the cytoplasm of the red blood

cell,
∗ in the cytoplasm, this is where the enzyme carbonic
1: carbonic anhydrase: an enzyme anhydrase 1 is found
found in the cytoplasm of red blood ∗ most of the hydrogencarbonate ions then diffuse out
Mr
cells that catalyses the reaction be- of the RBC into the blood plasma
tween CO2 & water to form carbonic ∗ in the blood plasma they are carried in solution
acid
2. 10% combined with haemoglobin, to form
carbaminohaemoglobin
∗ some CO2 diffuse into red blood, but do not

undergo a reaction catalysed by carbonic anhydrase
∗ CO2 combines directly with the amino group at the

end of each polypeptide chain of Hb
∗ to form carbaminohaemoglobin compound
∗ the amount of CO2 that can be carried depends on
the amount of O2 already being carried
∗ when it reaches the lungs, the above reaction goes in
reverse
3. 5% in solution in blood plasma
∗ most will be in physical solution
∗ a small amount will be carried as carbonic acid
(𝐻2 𝐶𝑂 3 )
§
7.4.5 Dissociation curve
§ the percentage saturation Hb in the blood is plotted against

the partial pressure of oxygen (pO2 )
§ it shows the affinity of Hb for oxygen
§ the higher the oxygen partial pressure, the greater the
oxygen saturation of Hb
• e.g in the lungs RBCs is rapidly loaded with oxygen
§ the oxygen dissociation curve has a sigmoid shape
§ over the steep part, a small decrease in oxygen pp of the
environment leads to a large fall in the percentage saturation
of Hb
• this means oxygen is released rapidly from Hb to diffuse
to cells
• the oxygen released is available to respiring tissues

curve for humans
§ at higher CO2 partial pressures, Hb gives up oxygen more

easily
§ the oxygen dissociation curve shifts to the right
§ this is important because
• in actively respiring tissues with a high (pCO2 ), Hb
2: Bohr shift: the decrease in affinity readily gives up its oxygen, this is called the Bohr shift 2
of haemoglobin for oxygen that oc- • in lungs with low (pCO2 ), oxygen binds easily to Hb
curs when CO2 is present
§ when CO2 dissolves in water it forms a weak acid
§ H2 O + CO2 Ý
âÝ
ÝÝ H2 CO3 Ý
á âÝ
Ýá
Ý H+ + HCO3–
water carbon dioxide carbonic acid hydrogen ion hydrogen carbonate ion
032
§ the hydrogen ions released combine with Hb making it less
able to carry oxygen
The chloride shift

214
733
§ the hydrogencarbonate ions that are produced inside red
blood cells, as a result of the action of carbonic anhydrase on
carbon b dioxide, diffuse out of the cells & into the blood
plasma
o0
§ these ions have a negative charge and, to balance their

movement, chloride ions (which also have a negative charge)
move from the blood plasma into the red blood cells
oy
3: chloride shift: the movement of § this is called the chloride shift 3

chloride ions into red blood cells § if the chloride shift did not happen, the inside of the red
from blood plasma, to balance a blood cell would develop an overall positive charge
F. M
the movement of hydrogencarbon- § because hydrogen ions (from the dissociation of carbonic
ate ions into the plasma from the
acid) would accumulate
red blood cells
§ hydrogen ions cannot leave the cell, because its cell
membrane is not permeable them
§ the influx of chloride ions therefore helps to prevent the
Mr
overall charge inside the cell from becoming too positive

7.5. CARDIAC CYCLE 91
7.5 Cardiac cycle
032
214
Figure 7.9: Pressure changes during
the cardiac cycle
§ it refers to a series of events occurring during one heartbeat

733
§ it involves contractions (systole) & relaxations (diastole) of
the heart
1. atrial diastole
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oy
F. M
Mr
Figure 7.10: Atrial diastole
• the atria & ventricles are relaxed

• blood returns to the heart at low pressure
• at first the bicuspid & tricuspid valves are closed

• as blood fills the atria, pressure increases &
• pressure in the atria becomes greater than pressure in
the ventricles
• the tricuspid & bicuspid valves open
2. Atrial systole
032
214
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F. M
Figure 7.11: Atrial systole
• the two atria then contract simultaneously

• this results in blood being pumped into the ventricles
3. Ventricular systole
Mr
032
214
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Figure 7.12: Ventricular systole

F. M
• the ventricles contract (ventricular systole)

• the pressure in the ventricles rises & closes the
atrioventricular valves
• this prevents blood from going to the atria
• pressure forces open the semi-lunar valves
Mr
• blood enters the aorta & pulmonary artery

• the closing of the of the atrioventricular valves produces
the first heart sound dub sound
4. Ventricular diastole
032
214
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Figure 7.13: Ventricular diastole

F. M
• after the ventricular systole, ventricles relax (ventricular

diastole)
• the high pressure in the aorta & pulmonary artery forces
some blood back towards the ventricles
• this closes the semi-lunar valves
Mr
• this produces the second heart sound (lub sound)
7.5.1 Myogenic stimulation of the heart
1 the sino-atrial node

• the heart has its own built-in mechanism for bringing
about contraction
• the stimulus originates in the SAN (sino-atrial node)
which is located in the right atrium
• the SAN is located near the vena cava & consists of a
small number of cardiac muscle fibres & a few nerve
endings from the autonomic nervous system
• the SAN is called the pacemaker because that is where

each waves of excitation begins
• during the atrial systole, the cells of the SAN become
slowly depolarised
• after some time, an action potential is set up in the cells
& a wave of excitation, similar to a nerve impulse passes
across the muscle fibres of the heart as the action
potential spreads from the SAN
• this causes both atria to contract simultaneously
• a layer of non conducting tissue (atrio-ventricular
septum) prevents the excitation from passing to the
032
ventricles
2 the atrio-ventricular node
214
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F. M
Figure 7.15: Myogenic stimulation
• the electrical activity from the SAN is picked by the AVN

• the AVN has a structure similar to the SAN
• the AVN then stimulates the bundle of His, a bundle of
Mr
tissue made up of fibres (Purkyne fibres)

• both ventricles are stimulated to contract simultaneously,
starting from the bottom of the heart & spreads upwards
7.5.2 Regulation of heart rate
§ basic heart rate is controlled by the SAN

§ the heart has to be adjusted to meet constantly changing
body demands
1 nervous control of heart rate
• the control centre is located in the medulla (located in
the hind brain)
• the cardiac inhibitory centre reduces the heart rate
• the cardiac accelerator centre stimulates the heart rate

• vagus nerves (which are parasympathetic nerves) go to
the SAN, AVN & bundle of His where they reduce heart
rate
• sympathetic nerves from the cardiac accelerator centre
go the SAN
• stimulation of these nerves increases the heart rate
• sensory nerves from the stretch receptors of the aortic
arch, vena cava & carotid sinus run to the cardiac
inhibitory centre
∗ impulses from the vena cava stimulate the heart
∗ impulses from the aorta & carotids inhibit the heart
2 hormonal control of heart rate
• adrenaline & noradrenaline stimulates the heart rate
• thyroxine increases metabolism which leads to increased
heart rate
7.5.3 Exercise & cardiovascular system
§ Short term effects

• there is increased blood flow, to supply raw materials &
remove wastes
• there is an increase in the output from the left ventricle
• this is due to increased heart rate & stroke volume
• this is brought about by the sympathetic nervous system
& adrenaline
• more of the body’s blood is pumped to the muscles
through shunting
∗ this when there is vasodilation in the muscles & vasoconstriction in
regions like intestines
• in the tissues maximum O2 is released

∗ CO2 released during respiration causes more O2 release due to the Bohr
effect
∗ high TC𝑂 around highly active muscles cause more unloading of O2
§ Long term effects

• the heart gets stronger
• there is an increased cardiac output
• the heart chambers increase in size
• the number & size of mitochondria increases
• blood supply to the lungs is increased
• there is improved efficiency of taking O2 from the
alveolus
§ The role of myoglobin
7.6. QUESTIONS 97
032
214
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curve for myoglobin
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• when muscles are very active p(O2 ) becomes very low

• the muscle then turns to oxymyoglobin
• myoglobin has a hyperbola-shaped dissociation curve,
oy
releasing O2 only in very low p(O2 )

F. M
7.6 Questions
Mr
032
1) The diagram shows pressure changes in various parts of the circulatory
214
one cardiac cycle.
733
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oy
F. M
At M & N, valves are either opening or closing.

Mr
a) With reference to the diagram, explain what is happening at M & N

b) Explain why the maximum pressure in the left atrium is lower than
pressure in the left ventricle.
2) The diagram shows the dissociation curves for fetal
haemoglobin in humans. The shape of the curves is describes
a) Explain the advantage, in terms of oxygen supply to the tissues, of t

maternal curve is sigmoid.
b) State the difference in percentage saturation of haemoglobin with o
maternal & fetal blood at an oxygen partial pressure of 4kPa.
c) Explain why it is essential for the survival of the fetus that the fetal
left of the maternal curve.
d) Describe the structure of arteries & explain how their structure is r
function.
8 Cell and nuclear division
032
8.1 Objectives
214 8.1 Objectives . . . . . . . 99
733
Objectives 8.2 Cell cycle . . . . . . . . 99
§ The Cell Cycle 8.3 Mitosis . . . . . . . . . 101
8.3.1 Interphase . . . . . . . 101
• outline the cell cycle
8.3.2 Prophase . . . . . . . . 102
• describe interphase
o0
8.3.3 Metaphase . . . . . . . 102

§ Mitosis 8.3.4 Anaphase . . . . . . . 102
• describe the behaviour of chromosomes, nuclear envelope, cell membrane, 8.3.5 Telophase . . . . . . . . 103
centrioles and spindles during mitosis
oy
8.4 Cytokinesis . . . . . . 103

• distinguish between cytokinesis in plants and animals 8.4.1 Animal cells . . . . . . 103
• explain the importance of mitosis 8.4.2 Plant cell . . . . . . . . 104
• identify factors that increase chances of cancerous growth 8.4.3 Differences between
F. M
• outline the stages involved in the development of cancer mitosis in plants &
§ Meiosis animals cells . . . . . . 105
• explain the meanings of the terms haploid, diploid and homologous
8.4.4 Importance of mitosis 105
chromosomes 8.4.5 Cancer . . . . . . . . . 106
• describe the behaviour of chromosomes, nuclear envelope, cell membrane, 8.5 Meiosis . . . . . . . . . 107
centrioles and spindles during meiosis 8.5.1 Meiosis I . . . . . . . . 108
Mr
• discuss the importance of meiosis 8.5.2 Meiosis II . . . . . . . . 111

• compare and contrast mitosis and meiosis 8.5.3 Significance of meiosis 113
8.5.4 Mitosis and meiosis . 113
8.6 Questions . . . . . . . 114
8.2 Cell cycle
§ this is a sequence of events between one cell division to the

next
§ it consists of interphase, cytokinesis & mitosis
§ cell divide regularly for growth & asexual reproduction
Interphase
100 CHAPTER 8. CELL AND NUCLEAR DIVISION
032
214
Figure 8.1: The cell cycle
§ it is a phase of non-division when cells increase in size and

mass, carry out normal activities & replicate their DNA
733
§ most of the time a cell is in interphase
§ the cell is carrying out its normal activities
§ it involves synthesis & growth
o0
§ synthesis of materials needed for growth & proper functions

§ there is DNA replication
§ it consists of G1 , S & G2 stages
G1 (gap 1) is a time between the previous mitotic division
oy
§
and chromosome replication
§ during G1 the cytoplasm increases in volume by producing
F. M
new proteins and cell organelles, including mitochondria

and endoplasmic reticulum.
§ during the G1 phase, the chromosomes are checked for
damage.
• if damage is detected, the cell does not proceed into the S phase until
Mr
the DNA has been repaired

§ during S phase, the DNA replicates ready for mitosis, so
there are two identical copies of each DNA molecule in the
nucleus
§ each DNA molecule forms one chromosome
§ after DNA replication, each chromosome consists of two
identical DNA molecules called chromatids that are joined
together at at centromere
§ G2 is when organelles needed for cell division are
synthesised
§ G2 replicated DNA is ‘double checked’ for errors and
corrected if any errors are found
§ cell growth continues by further synthesis of proteins and
cell organelles
8.3. MITOSIS 101
§ the length of interphase differs depending on the role of the

§ the S and G2 phases of most cells remain relatively constant
in duration
§ the length of the G1 phase is more variable; some cells can
take weeks, months or even years to complete this phase
§ during interphase, the individual chromosomes are
unravelled
DNA levels in dividing cells
§ the mass of DNA in a cell can be measured using a technique
032
called flow cytometry
§ a fluorescent dye that binds to nucleic acids is added to cells
and then the level of fluorescence is measured – the more
fluorescence, the more DNA is present
214
§ the cells are treated with the enzyme RNAase, which
removes RNA, before carrying out the flow cytometry.
§ the readings are calibrated by reference to the nucleated red
blood cells of chickens, because the mass of DNA in those
733
cells is known
Mitosis
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§ it is a process of nuclear division Figure 8.2: The cell cycle

§ one nuclear nucleus divides to from 2 identical daughter
nuclei
oy
F. M
Cytokinesis
§ this involves division of the cytoplasm
8.3 Mitosis
Mr
8.3.1 Interphase
§ DNA replication occurs

§ each chromosome exists as a pair of chromatids
§ sister chromatids are joined by a centromere
Figure 8.3: Interphase

§ the chromosome number is 4n

§ centrioles have replicated
§ chromosome material is loosely coiled chromatin
8.3.2 Prophase
§ chromosomes shorten and thicken

§ by coiling & tighter packaging of the components
§ chromosomes become visible during prophase, because the
Supercoiling The twisting of the DNA DNA undergoes supercoiling
around its own axis, winding the § centrioles move to opposite poles of the cell (in animal cells)
032
helix more tightly. § asters (microtubules) start radiating from the centrioles
§ the nucleoli disappears
§ the nuclear envelope disappears
214
§ spindle is formed
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Figure 8.4: Prophase

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8.3.3 Metaphase
oy
§ chromosomes line up around the spindle equator

§ spindles bind chromosomes at the centromeres
F. M
Mr
Figure 8.5: Metaphase
8.3.4 Anaphase
§ centromeres split into two

§ spindle fibres pull daughter centromeres to opposite poles
§ separated chromatids are pulled along behind centromeres
8.4. CYTOKINESIS 103
Figure 8.6: Anaphase
8.3.5 Telophase
§ chromatids reach opposite poles
032
§ chromatids uncoil & lengthen to form chromatin
§ they are nolonger clearly seen
§ spindle fibres disintegrate
§ centrioles replicate
214
§ nuclear envelope re-forms around chromosomes at each pole
§ the nucleoli reappears 733
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Figure 8.7: Telophase

oy
8.4 Cytokinesis
F. M
§ it is the division of the cytoplasm

§ cell organelles become evenly distributed towards the 2 poles
8.4.1 Animal cells

Mr
§ cell surface membrane invaginates during telophase

§ invagination occurs where there was the spindle equator
§ this is due to microfilaments in the region
§ this forms a furrow around the outside surface of the cell
§ cell surface membrane in the furrow joins up
§ and separate the two cells
Figure 8.8: Cytokinesis in animal

cells
032
8.4.2 Plant cell
214
§ spindle fibres disappear during telophase everywhere,
except in the spindle equator
§ they move outward in diameter
§ they increase in number
733
§ they for a phragmoplast
§ a barrel-shaped region
§ microtubules, ribosomes, microtubules, GA, ER, are attached
to this region
o0
§ GA produces many small fluid-filled vesicles

§ the vesicles are guided by microtubules
§ they fuse to form a cell plate
oy
§ cell plate grows across the equatorial plane

§ vesicle contents form middle lamella and cell wall of
daughter cells
F. M
§ vesicle membrane form new surface membrane

§ new cell walls are primary cell walls
§ they thicken by addition of cellulose, lignin & suberin
§ to form secondary cell wall
§ in some areas vesicles don’t fuse
Mr
§ they leave gaps, the plasmodesmata

8.4. CYTOKINESIS 105
032
214
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Figure 8.9: Cytokinesis in plant cells

oy
8.4.3 Differences between mitosis in plants & animals

cells
F. M
Plant cell Animal cell

Table 8.1: Differences between mito-
no centriole present centriole present
no aster formation aster forms sis in plants & animals cells.
cytokinesis has plate formation cytokinesis has furrowing & cleavage
of cytoplasm
occurs mainly at meristem occurs in tissues throughout the body
Mr
8.4.4 Importance of mitosis
Genetic stability
§ two identical daughter nuclei are produced

§ they have the same chromosome number as the parent cell
§ this is because they were derived from the same parental
DNA
§ produced through faithful copying of parental chromosomes
§ their genes have the same hereditary information
§ daughter cells are genetically similar/identical to parent cell
§ there is no variation in genetic information
§ genetic stability within populations
Growth
§ mitosis leads to an increase in cell number

§ basis of growth in multicellular organisms
Cell replacement
§ cells are dying constantly

§ they are replaced by cells from mitosis
Regeneration
032
§ some animals can regenerate lost tissues
§ using cells produced by mitosis
214
Asexual reproduction
§ asexual reproduction relies on mitosis

733
8.4.5 Cancer
§ a result of uncontrolled cell division or mitosis

o0
§ it is due to mutations
§ also due to activation of genes which control cell division
§ abnormal genes called oncogenes
oy
§ one cell divides to from a tumour (primary tumour)

§ a tumour is a mass of undifferentiated cells
§ a primary tumour can break away (metastasis) to form a
F. M
secondary tumour else in the body (metastases)

§ it is transported by blood or lymphatic system
§ tumours that spread leading to ill health & death are
malignant
§ tumours that do not spread are benign
Mr
Causes of cancer
§ factors which lead to mutations are mutagens

§ agents which cause cancer are carcinogens
Retroviruses
§ these are RNA viruses

§ they invade body cells & manufacture copies of viral DNA
§ using reverse transcriptase
§ then DNA is inserted into host DNA
§ same cause cancer by altering host cell division genes
§ they switch them on & causing the cell to become malignant
8.5. MEIOSIS 107
DNA viruses
§ some viruses have DNA as their hereditary material

§ some contain oncogenes which result in uncontrolled cell
division of host cells
§ e.g papilloma viruses
Hereditary predisposition
§ some cancers run in the family

§ genes responsible may be oncogenes
§ or genes which lead to failure to kill cancer cells
032
§ e.g breast cancer
UV light
214
§ DNA absorbs UV light
§ the energy is used in converting the bases into more reactive
forms
733
§ the reactive forms react with surrounding molecules
§ sunlight contains UV light & prolonged exposure to it can
result in skin cancer
o0
Radon gas
§ it is radiation released by some rocks e.g granite

oy
§ it may accumulate in houses or areas where rocks are found

F. M
Chemical mutagens
§ e.g tobacco smoke & some foods
8.5 Meiosis
Mr
§ it normally produces 4 haploid daughter cells

§ it involves two divisions, meiosis I and meiosis II
§ it produces daughter cells that have half the number
chromosomes as the parent cell
§ it occurs during gametogenesis in animals and spore
formation in plants
§ it produces daughter cells that are genetically different lves
two divisions, meiosis I and meiosis II
§ during interphase, before meiosis, chromosomes have been
replicated to form two chromatids held by their centromeres
§ at the end of meiosis I, homologous chromosomes have been
separated into two new cells
§ sister chromatids are separated during meiosis II
8.5.1 Meiosis I
§ preceded by interphase
§ interphase is similar to that preceding mitosis
§ DNA & organelles are duplicated & energy is stored as ATP
§ homologous chromosomes pair up & their chromatids wrap
around each other
§ equivalent portions of these chromosomes may be
exchanged during crossing over
032
§ by the end of meiosis I homologous pairs have separated
§ with one chromosome from each pair going into one of the
two daughter cells
214
Prophase I
§ chromosomes condense
733
• they supercoil to become shorter & thicker & become visible in the
light microscope
§ homologous chromosomes pair up (synapsis) to form
bivalents containing four chromatids
o0
§ the chromatids is each bivalent break & rejoin to form

chiasmata or crossovers
• this is where sectors of non-sister chromatids can be exchanged
oy
§ nuclear membrane breaks up to form small membrane sacs

§ the centriole replicates & migrates to opposite poles of the
F. M
cell
§ centriole forms spindle fibres
Metaphase I
Mr
§ microtubules attach from the centrioles to the centromere of

each chromosome
§ bivalents move to the equator of the cell
8.5. MEIOSIS 109
032
214
733
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oy
F. M
Mr
Figure 8.10: Overview of meiosis

032
214
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F. M
Figure 8.11: Prophase I

Mr
8.5. MEIOSIS 111
§ orientation of each bivalent on the equator is random

• maternal or paternal chromosomes could be facing either pole
Anaphase I
§ microtubules shorten to separate the homologous

chromosome (each with two chromatids) Figure 8.12: Metaphase I
§ homologous chromosomes are pulled towards opposite
poles
§ each chromosome still consists of two chromatids
032
§ the sister chromatids of each chromosome move as a single
unit
§ centromeres do not divide
§ chromosomes number in each cell is half that of the original
Telophase I
§ chromosomes reach opposite poles 214 Figure 8.13: Anaphase I

733
§ nuclear membrane reforms around each set of chromosomes
§ this produces two nuclei
§ these nuclei are haploid
o0
§ the cell membrane pinches to from two cells (cytokinesis)

§ in animals & some plants the chromatids usually uncoil
§ the nucleus enters interphase
in many plants there is no telophase
oy
Figure 8.14: Telophase I

F. M
Interphase II
§ usually in animals cells only

§ no further DNA replication occurs
8.5.2 Meiosis II
Mr
§ similar to mitosis
§ results in separation of sister chromatids
Prophase II
§ centrioles replicate & move to poles that are at right angles to

those in meiosis I
§ nuclear membrane breaks up
Figure 8.15: Prophase II
Metaphase II
§ individual chromosomes align at the equator
032
§ chromatids are randomly aligned at the equator
§ microtubules attach to the centromeres
214
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Figure 8.16: Metaphase II
Anaphase II
o0
§ sister chromatids break apart at the centromere & move to

opposite poles
oy
F. M
Figure 8.17: Anaphase II

Mr
Telophase II
§ nuclear membrane reforms

§ cytokinesis occurs to produce four genetically different
haploid cells
§ spindle fibres disappear & centrioles replicate
Figure 8.18: Telophase II

8.5. MEIOSIS 113
8.5.3 Significance of meiosis
1 Sexual reproduction
• it occurs in all organisms which carry out sexual
reproduction
• to produce a gamete with a haploid number of
chromosomes
• when haploid gametes fuse a diploid zygote is produced
• if meiosis did not occur it would result in doubling of

chromosome number
2 Genetic variation
• it provides an opportunity for new combinations of
genes to occur in the gametes
• this gives rise to genetic variation of offspring
i) independent assortment of chromosomes
∗ the chromosomes that came into the individual’s two parents
are distributed into gametes completely at random
∗ the orientation of bivalents at the equator in metaphase I is
random
∗ chromosome in each bivalent separate /assort independently of
other bivalents during anaphase I
ii) crossing over
∗ each chromosome in a homologous pair carries !h
genes for the same characteristic at the same locus
∗ alleles of the genes on two chromosomes may be the
same or different
∗ during prophase I, two homologous chromosomes
lie side by side & their chromatids may form links
called chiasmata
∗ there is crossing over of segments of chromatids
between homologous chromosomes during
prophase I
∗ the points where chromatids break are called
chiasmata
∗ when they move apart a piece of chromatid from
one chromosome may swap places with a piece
from the other chromosome
∗ this leads to the formation of new combinations of
genes on the chromosomes of the gametes
Figure 8.19: Crossing over

8.5.4 Mitosis and meiosis
Table 8.2: Differences between mitosis & meiosis
Mitosis Meiosis
prophase
§ homologous chromosomes re- § homologous chromosomes
main separate pair up
§ no formation of chiasmata § chiasmata form
§ no crossing over § crossing over may occur
metaphase
§ chromatid pairs line up at the § chromosome pairs line up at
equator the equator
anaphase
032
§ centromeres divide § centromeres do not divide
§ chromatids separate § whole chromosomes separate
§ separating chromatids identi- § separating chromosomes &
cal chromatids may not be iden-
tical due to crossing over
214
telophase
§ same number of chromosomes § half the number of chromo-
present in daughter cells as par- somes present in daughter cells
733
ent cells § only one of each pair of homol-
§ both homologous chromo- ogous chromosomes present in
somes present in daughter cells daughter cells
if diploid
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occurrence
§ may occur in haploid, diploid § only occurs in diploid or poly-
or polyploid cells ploid cells
§ occurs during formation of so- § occurs during formation of ga-
oy
matic cells & some spores metes or spores

§ also occurs during gamete for-
mation in plants
F. M
8.6 Questions
Mr
8.6. QUESTIONS 115
1) Fig 8.20 indicates the appearance of a chromosome at early prophase of mitosis.
a) With reference to 8.20,

i) name structure A; [1]
ii) explain why two chromatids are identical. [2]
Fig 8.21 represents the nucleus of an animal cell (2n=6) at early prophase of mitosis.
032
214
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b) Re-draw Fig 8.21 and shade one pair of homologous chromosomes. [1]
c) In the space below, draw an annotated diagram to indicate what happens in this
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cell at anaphase of mitosis. [4]

d) i) State the number of chromosomes which would be found in a haploid cell in
this animal. [1]
ii) Explain why haploid cells need to be produced during a life cycle which
includes sexual reproduction. [3]
2) Some cells divide by mitosis.
Mr
a) i) Describe the products of mitosis. [2]

ii) State two processes in which mitosis occurs in humans. [2]
A gorilla has a diploid number of 48
b) State the number of chromosomes which would be found in the following cells of
the gorilla
- brain cell
- epithelial cell
- sperm
- muscle cell [4]
Cancer is caused by uncontrolled mitotic cell division.
d) State three factors which can increase the chances of cancerous growth. [3]
Figure 8.21
Mr
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214
032
9 Genetic control
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This chapter contains notes on genetic control.
214 9.1 Objectives . . . . . . . 117
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9.2 Nucleic acid . . . . . . 117
9.1 Objectives 9.2.1 Nucleotides . . . . . . 118
9.2.2 Polynucleotides . . . . 119
Objectives 9.3 Replication of DNA . 123
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9.3.1 Protein synthesis . . . 127

§ Nucleic Acids 9.4 Questions . . . . . . . 133
• describe the structure of a nucleotide
• describe formation of a dinucleotide
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• distinguish between Ribonucleic acid (RNA) & Deoxyribonucleic acid

(DNA) nucleotides
§ Structure and replication of DNA

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• describe the structure of DNA

• explain how DNA replicates
§ Protein synthesis
• outline the process of protein synthesis
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9.2 Nucleic acid
§ nucleic acids are RNA1 & DNA2 1: Ribonucleic acid is a single-

§ they are the genetic code in all living things stranded polymer of nucleotide
§ they control cellular activity and protein synthesis molecules containing the pentose
§ they are made up of carbon, hydrogen, oxygen, nitrogen & sugar ribose. There are three types
of RNA.
phosphorous
2: Deoxyribonucleic acid is a double-
§ they are made up of units called nucleotides
stranded polymer of nucleotide
§ nucleotides are arranged to form long molecules called
molecules that carries the informa-
polynucleotides tion for protein synthesis. It contains
the pentose sugar deoxyribose.
118 CHAPTER 9. GENETIC CONTROL
9.2.1 Nucleotides
§ it has three components a 5 carbon (pentose) sugar,

nitrogenous base & phosphoric acid
§ the sugar can be a ribose [in RNA] or deoxyribose [in DNA]
(ribose with an oxygen atom removed from carbon atom 2)
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214
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Figure 9.1: Pentose sugar
3: Nucleotides are monomers from § there are four different bases in a nucleotide 3 , two purines &
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which nucleic acids are formed. two pyrimidines

They are a combination of a phos- § the nitrogen in the bases gives the molecule their basic
phate, a pentose sugar and an or- structure
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ganic base.
§ the purines are adenine (A) & guanine (G)
§ the pyrimidines are cytosine (C) & thymine (T) [in DNA] or
uracil (U) [in RNA]
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§ purines have two rings

§ pyrimidines have one ring
§ phosphoric acid gives nucleic acid their acid character
§ a sugar & base combine through a condensation reaction to
from a nucleoside
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§ a nucleoside & phosphoric acid combine through a

condensation reaction to from a nucleotide
§ nucleotides are building blocks of nucleic acids, coenzymes
e.g ATP, cAMP, NAD, NADP, FAD
ure 9.3: Nucleotide
Figure 9.4: Nucleotide

9.2. NUCLEIC ACID 119
9.2.2 Polynucleotides
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214 Figure 9.5: Dinucleotide
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§ two nucleotides join to form a dinucleotide
§ this is by a condensation reaction between the phosphate
group of one nuclei acid with the sugar of the other nucleic
acid
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§ the bonds are formed by condensation and are called

phosphodiester bonds
§ they can be broken by hydrolysis.
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§ the process is repeated several times to make a

polynucleotide 4 4: Polynucleotide - A polymer of
nucleotide monomers covalently
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bonded together.
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Figure 9.6: Dinucleotide
Structure of DNA
§ it stores all of the genetic information needed by an

organism, which is passed on from generation to generation
§ it consists of two polynucleotide chains
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214
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Figure 9.7: Base pairing
each chain forms a right-handed helical spiral

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§
§ two chains coil around each other to form a double helix
§ the chains run in opposite directions, they are antiparallel
§ each chain has a sugar-phosphate backbone
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§ bases of opposite chains form hydrogen bonds across the

double helix
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§ the double helix is 2 nm wide

§ bases are 0.34nm apart
§ a complete turn of the double helix is 3.4 nm & 10 base pairs
§ the two chains are complementary
§ bases always pair up in a specific way
•
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a purine always joins with a pyrimidine

• T pairs with A, G pairs with C
• A & T have two hydrogen bonds
• G & C have three hydrogen bonds
§ complementary base pairing is key to;
1 the stability of the DNA double helix, because millions
of hydrogen bonds in DNA molecule provide strength
2 the way is which genetic information can be transferred
from DNA to RNA
3 the way amino acids are assembled into polypeptides in
Figure 9.8: Structure of DNA
the cytoplasm
9.2. NUCLEIC ACID 121
032
214 Figure 9.9: Structure of DNA
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Structure of RNA
§ it plays an essential role in the transfer of genetic material

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from DNA to proteins

§ it is normally single stranded
§ tRNA & rRNA can assume complex structures
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§ there are three types of RNA; mRNA, tRNA & rRNA

§ all three types of RNA are synthesised directly on DNA
§ the amount of RNA in a cell is directly related to the amount
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of protein synthesis
Messenger RNA
§ it accounts for about 3-5% of the total RNA in a cell

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§ it is made up by attaching RNA bases to a short section of

unzipped DNA
§ RNA nucleotides attach to the exposed DNA bases with
hydrogen bond building mRNA
§ only one strand of DNA is used in the formation of mRNA
§ complementary base pairing means that the correct bases are
always attached
§ mRNA copies information from the DNA code - this is
transcription 5 5: Transcription - the process of copy-
ing the code exactly from DNA to
form a template of mRNA
Transfer RNA
§ it makes about 15% of total RNA in a cell

§ they are short chains of RNA that fold on themselves to form

some parts that are doubled
§ they are clover-shaped molecules
§ they carry amino acids to the mRNA & ribosomes during
protein synthesis
§ each amino acid has its own family of tRNA molecules
§ it is the smallest RNA
§ all tRNAs molecules have the same basic structure
§ one part of tRNA has a sequence of three bases that matches
the genetic code of the DNA & corresponds to one particular
amino acid anticodon
Figure 9.10: Structure of tRNA
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§ each tRNA has a binding side with which it picks up one
particular amino acid
214
Ribosomal RNA
§ it makes about 80% of total RNA in a cell

§ it is synthesised by genes in chromosomes found in the
nucleolar organised which is found in the nucleolus
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§ they are short chains of RNA
§ the base sequence of rRNA is similar in all organisms
§ it is found in the cytoplasm
they are attached to ribosomal proteins to form ribosomes
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§
§ they are the site of protein synthesis
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DNA & RNA
Table 9.1: Differences between DNA

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and RNA
Feature DNA RNA
Basic double strand single strand

shape
Nitrogenous adenine, thymine,cytosine & gua- adenine, uracil, cytosine and gua-
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bases nine nine

Type of deoxyribose ribose
pentose
sugar
Helical na- a double helix of two antiparallel one polynucleotide chain twists into
ture of the polynucleotide chains a helix & coils back on itself
molecule
Types of one type three types, mRNA, tRNA, rRNA
molecule
Role long term storage of genetic infor- protein synthesis
mation
Ratio of A:T = 1:1; C:G=1:1 A+G : C+G = A:G is ‰ 1:1; C:U is ‰ 1:1
base pairs 1+1
9.3. REPLICATION OF DNA 123
9.3 Replication of DNA
§ new DNA molecules need to be made before a cell can divide

§ the two daughter cells must each receive a complete set of
DNA
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214
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Figure 9.11: The process of DNA replication.
§ the base sequences on the new DNA molecules must be

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identical with those on the original set

a The two strands of the DNA molecule begin to unwind
when the weak hydrogen bonds between bases break.
• This happens at the point where the DNA is to be
copied.
b Free DNA nucleotides pair with complementary bases
that are exposed on the unwound DNA.
c Hydrogen bonds form between the new nucleotides and
bases of each polynucleotide strand.
d At each DNA strand, the enzyme DNA polymerase joins
the free nucleotides together. Each new strand is an
exact copy of one of the old strands.
§ DNA Replication means to make an identical copy replication
takes place in the nucleus, during interphase
032
214
Figure 9.12: Three different theories
of DNA replication
1 Hydrogen bonds between the bases along part of the

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two strands are broken
• this ‘unzips’ part of the molecule, separating the two
strands.
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2 nucleotides that are present in solution in the nucleus

are moving randomly around
• by chance, a free nucleotide will bump into a newly
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exposed one with which it can form hydrogen bonds

• free nucleotides therefore pair up with the nucleotides
on each of the DNA strands, always A with T and C
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with G
3 DNA polymerase links together the phosphate and
deoxyribose groups of adjacent nucleotides.
• this is called semi-conservative replication, because each
new DNA molecule has one old strand and one new one.
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Semi-conservative DNA replication
6: Semi-conservative replication § it is called semi-conservative 6 DNA replication

means that half of the original § because each new double helix retains (conserves) one of the
molecule is conserved in each of the two original DNA strands
new molecules. § DNA double helix unwinds & the hydrogen bonds between
base pairs break
§ it is controlled by DNA helicase
§ the polynucleotide chains separate, exposing the bases
§ each strand is then used as a template to make two new
double strands
7: DNA polymerase: an enzyme that § the enzyme DNA polymerase 7 then binds to the single
copies DNA; it runs along the sep- stranded DNA
arated DNA strands lining up one
complementary nucleotide at a time
ready for joining by DNA ligase
§ the enzyme starts to move along the strand

§ each time it meets a base on the DNA
1) free nucleotides approach the DNA strand
2) the one with the correct complementary base
hydrogen-bonds to the base in the DNA
3) the free nucleotide is then held in place by the enzyme
until it binds to the preceding nucleotide by a
condensation reaction
4) thus extending the new DNA strand
§ the enzyme continues to move along one base at a time
§ the new DNA strand grows as it does so
032
§ this movement can only happen in the 5‘ Ñ 3‘ direction
§ this means that only one strand (leading strand) 8 can be
copied continuously
§ because the DNA polymerase is moving in the same
214
directions as the unwinding enzyme
§ this is called continuous replication
§ the copying of the other strand (lagging strand) 9 has to keep
being started again
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§ because the DNA polymerase has to move away from the
unwinding enzyme
§ this results in small gaps being left because the DNA
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polymerase cannot join the 3‘ end of one newly synthesized Figure 9.13: DNA polymerase only
DNA to the 5‘ travels in the 3’ to 5’ direction only
§ these short DNA fragments are called the Okazaki fragments 8: leading strand: during DNA repli-
DNA ligase 10 joins the Okazaki fragments
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§ cation, the parent strand that runs

§ this is called discontinuous replication in the 3 to 5 direction is copied to
§ once completed each daughter DNA molecule rewinds into a produce the leading strand
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double helix 9: lagging strand: during DNA repli-

§ DNA polymerase also has a role in ‘proof reading’ the new cation, the parent strand that runs
strands in the 5 to 3 direction is copied to
§ any ‘mistakes’ that start to happen (for example, the wrong produce the lagging strand
bases pairing up) are corrected 10: DNA ligase: an enzyme that catal-
yses the joining together of two nu-
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§ as a result, each new DNA double helix is an exact copy of

the original. cleotides with covalent phosphodi-
ester bonds during DNA replication
Meselson & Stahl experiment
§ E. coli was cultured for many generations in a medium where

their only nitrogen source was the heavy radioactive isotope
15
𝑁 from 15 𝑁 𝐻4 𝐶𝑙
§ all the DNA became labelled 15 𝑁
§ the cells were transferred to a medium with normal 14 𝑁 &
allowed to grow
§ the cells were left for times equal to generation time of E. coli
§ samples of cells were removed & DNA extracted &
centrifuged at x 400 000 gravity in a solution of caesium
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Figure 9.14: DNA replication
chloride (CsCl)
§ DNA settled & formed bands which were viewed under UV
light
§ these experiments demonstrated that DNA is
semi-conservative
• When DNA from labelled cells was extracted and
centrifuged in a density gradient (of different salt
solutions) all the DNA was found to be ‘heavy’.
• In contrast, the DNA extracted from cells of the original

culture (before treatment with 15 𝑁 was ‘light’
• after one generation all the DNA was of intermediate
density (each of the daughter cells contained (i.e.
conserved) one of the parental DNA strands containing
15
𝑁 alongside a newly synthesised strand containing
DNA made from 14 𝑁
• after two generations 50% of the DNA was intermediate
and 50% was ‘light’. This too agreed with
semi-conservative DNA replication, given that labelled
DNA was present in only half the cells (one strand per
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cell).
9.3.1 Protein synthesis
214
§ DNA directly synthesises proteins
§ the proteins can have a structural role e.g keratin & collagen
or functional roles e.g enzymes, insulin, fibrinogen
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§ it is the particular enzymes in a cell which determine the
type of cell it becomes
• this is the way DNA controls the activities of a cell
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§ protein synthesis is a 2-stage process

1) transcription - the making of mRNA from DNA
2) translation - translation of the base sequences in mRNA
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into an amino acid sequence in a protein

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Transcription
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Figure 9.16: Transcription
§ mechanism by which the base sequence of DNA

representing a gene is converted into the complementary
base sequence of mRNA
§ DNA double helix unwinds by breakage of hydrogen bonds
between bases of two strands
§ only one of the DNA strands is used as a template for the
formation of a complementary mRNA
§ mRNA is formed by linking free nucleotides under the

catalysis of RNA polymerase
§ RNA polymerase moves in the 3’ Ñ5’ direction
§ RNA polymerase catalyses the formation of phosphodiester
bonds on the mRNA phosphate backbone
§ mRNA molecules once formed leaves the nucleus via nuclear
pores
§ the DNA strands zip up to reform the double helix
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214
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Figure 9.17: Transcription

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§ the mRNA formed is called pre-mRNA

§ it contains both introns & extrons
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§ introns are spliced out to produce mature mRNA

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214
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Figure 9.15: A summary of the experiment carried out by Meselson and Stahl
Table 9.2:DNA RNA between

Comparison
strand strand
replication & transcription
Features Replication Transcription
A U
C G DNA unwinds & hydro- X ˆ
gen bonds within DNA
G C break
T A number of polynu- 2 1
cleotide strands that
act as template
free activated nu- X DNA nucleotides ˆ RNA nucleotides
032
cleotides align against
DNA
bases of free nu- A, G, C, T A, G, C, U
cleotides
214
base pairing A-T, T-A, G-C, C-G (per- A-U, T-A, G-C, C-G
manent) (temporary)
enzyme catalysing syn- DNA polymerase RNA polymerase
thesis
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type of nucleotide pro- DNA RNA
duced
quantity of DNA in- all the DNA in the nu- only the DNA of the
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volved cleus genes that are active at

the time
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Translation
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214
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Figure 9.18: Summary of translation

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§ mechanism by which the sequence of bases in mRNA is

converted into a sequence of amino acids in a polypeptide
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chain
§ it occurs on ribosomes
§ several ribosomes may be attached to a molecule of mRNA to
F. M
from a polysome or polyribosome

• this allows several polypeptides to be synthesised at the
same time
§ each ribosome is composed of small & a large subunit
§ the first two codons at the 5‘ enter the ribosomes
Mr
§ the first codon binds the aminoacyl-tRNA molecule having

the complementary anticodon & which is carrying the first
amino acid (usually methionine)
§ the starting codon on mRNA is normally AUG
§ the second codon attracts an aminoacyl-tRNA molecule
showing the complementary anticodon
§ the ribosomes hold in position the mRNA, tRNA &

associated enzymes until a peptide bond forms between
adjacent amino acids
§ after adding a new amino acid, the ribosome moves one
codon along the mRNA
§ the tRNA molecule which was previously attached to the
polypeptide chain leaves the ribosome & goes to the
cytoplasm to form another aminoacyl-tRNA molecule
§ this continues until a stop codon or terminating codon is
reached, usually UAA, UAG or UGA
§ the polypeptide leaves the ribosomes & translation is
complete
9.4. QUESTIONS 133
§ the polypeptide may immediately fold into its secondary,

tertiary & quaternary structure
§ if translation occurs on the RER, the protein enters the RER
to be transported
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9.4 Questions
214
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214
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1) a) i) Name the sugar in DNA. [1]
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ii) State how many carbons this sugar contain. [1]
iii) How is this sugar similar & different to that found in RNA? [2]
b) State the name of the nitrogenous base which
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i) is present in DNA but not in RNA.
ii) is present in RNA but not in DNA.
The diagram represents part of the process of protein
[1]
[1]
synthesis.
F. M
Mr
c) With reference to the diagram, name

i) the type of RNA present in the structure labelled A [1]
ii) the two types of RNA labelled B and C. [2]
iii) structures D to F. [3]
iv) the bond linking structures labelled F in the polypeptide chain. [1]
d) Explain how the sequence of bases in DNA determines the order of amino acids in
a polypeptide chain. [4]
2) Describe how DNA replicates. [8]
10 Inherited change & evolution
032
This chapter contains notes on inherited change & evolution.
214 10.1 Objectives . . . . . . 135
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10.2 Nature of genes . . . 135
10.1 Objectives 10.2.1 Genes . . . . . . . . . 135
10.2.2 The nature of genes . 136
Objectives 10.3 Genetic crosses . . . 136
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10.3.1 Monohybrid crosses 136

§ Nature of gene 10.3.2 Dihybrid crosses . . 143
• discuss the gene concept 10.3.3 Chi squared tests . . 146
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§ Monohybrid & dihybrid crosses 10.4 Questions . . . . . . . 150

• use genetic diagrams to solve problems involving monohybrid & dihybrid
crosses
F. M
• use chi – squared test to test the significance of difference between

observed & expected results
10.2 Nature of genes

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10.2.1 Genes
§ genetics is the study of how characteristics that are

determined by genes are passed down from a parent or
parents to their offspring.
§ the sequence of bases in a DNA code that determines the
sequence in which amino acids are linked together making a
protein molecule
§ it is a unit of inheritance
§ it is a unit of recombination
• it is the shortest segment of a chromosome which could
be separated from adjacent segments by crossing-over
136 CHAPTER 10. INHERITED CHANGE & EVOLUTION
§ it is a unit of function
• it is the shortest segment of a chromosome responsible
for the production of a specific product
• it is a piece of DNA which codes for a protein
§ the gene is found at the same locus on the same chromosome
§ different forms of the same are called alleles each with a very
slightly different nucleotide bases
10.2.2 The nature of genes
§ the code is a triplet code
032
• three bases in DNA code for one amino acid
• the code is first copied to mRNA
• the complementary triplets in mRNA is the codon
214
§ the code is degenerate
• some amino acids are coded for by several codons
§ the code is punctuated
• some codons act as stop codons
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• some codons act as start codons
§ the code is universal
• all organisms have 20 common amino acids
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• all organisms have the same five bases

§ the code is non-overlapping
• AUGAGCGCA is not read as AUG-UGA-GAG or AUG-GAG-GCG
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but it is read as AUG-AGC-GCA

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10.3 Genetic crosses
10.3.1 Monohybrid crosses

Mr
Genotype & phenotype
Figure 10.1: Different allele combinations

10.3. GENETIC CROSSES 137
§ every body cell contains two copies of each type of

chromosome called homologous chromosomes
§ every cell contains two copies of every gene
§ there are different combinations of the alleles of this gene,
the genotype 1 1: genotype: the alleles possessed by
§ the genotype is the genetic make-up of an organisms an organism
§ the genotype sets describe all the alleles that an organism
contains
§ a genotype in which both alleles are the same is said to be
homozygous 2 . 2: homozygous: having two identical
§ a genotype in which the two alleles are different is alleles of a gene
heterozygous 3
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3: heterozygous: having two different
§ the observable characteristics of an organism are called its alleles of a gene
phenotype 4 4: phenotype: the observable features
§ the phenotype is as a result of the interaction between the of an organism it is affected by genes
214
expression of the genotype & the environment & also by environment
§ lets imagine a gene controlling pod colour in peas
• the gene has 2 alleles
• one allele for green pods
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• one allele for yellow pods
• if a pod has two alleles for a green pods in the genotype
(homozygous) it will have a phenotype of green pods
• if a pod has two alleles for a yellow pods in the genotype
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(homozygous) it will have a phenotype of yellow pods

• if alleles for green pods & yellow pods are present
(heterozygous) in the genotype, the phenotype is always
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green pods
§ the allele of the heterozygote that expresses itself in the
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phenotype is said to be dominant

§ the allele of the heterozygote that does not expresses itself in
the phenotype is said to be recessive
§ a homozygous organism with two dominant alleles is said to
be homozygous dominant
Mr
§ a homozygous organism with two dominant alleles is said to

be homozygous recessive
§ the effect of a recessive allele is apparent when it occurs in
the presence of another identical allele
§ in some cases, two alleles both contribute to the phenotype
in which case they are referred to as co-dominant5 5: co-dominance: When two alleles
§ when both alleles occur together the phenotype is either a of the same gene influence the phe-
blend of both features or both features present notype of a heterozygous organism
because both are dominant over any
• the presence of both A & B antigens produces blood
other alleles of the gene but neither
group AB - alleles occurring together
allele is dominant over the other.
• imagine a gene for coat colour in rabbit with an allele for
black colour & white colour
• when a black allele occurs with a white allele, a brown
coat is produced - a blend
6: incomplete dominance: When nei- § a monohybrid cross may also involve incomplete dominance 6
ther of two alleles of a gene domi- § in such cases neither allele is dominant, although they are
nates so there is blending of the two both present at the same gene locus
to form an intermediate § the phenotype is a mixture of the effects of the two alleles.
• for example, if two alleles for petal colour in flowers
were red & white, the heterozygote would be pink.
Figure 10.2: Full genetic cross
Monohybrid inheritance
§ There are a number of basic considerations to follow when

drawing genetic diagrams.
• Always start with the parental phenotypes & follow
with the parental genotypes where known.
• When there are two alleles at a locus, one dominant &
one recessive, always aim to represent a gene by a single
letter.
∗ In some cases a second may be added to avoid
confusion.
∗ Use upper case for the dominant allele & lower case Construct a genetic diagram
for the recessive allele. to predict the chance that a
∗ Choose a letter that is easily distinguished. child born to two parents,
• If a gene has more than two alleles (multiple alleles) in both with blood group AB,
the population use a single upper-case letter for the gene will have blood group B. Use
the symbols I𝐴 & I𝐵 to repre-
& superscript letters for the alleles.
sent the alleles.
∗ For example, the human ABO blood groups use I for
the gene with the alleles given as I𝑂 , I𝐴 & I𝐵 .
• Co-dominance may be shown with the gene in upper
case & the co-dominant alleles as superscript letters (as
for the A & B blood groups, I𝐴 & I𝐵 ).
032
214
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Figure 10.3: Cross between F1 pea

plants using a punnet square
Co-dominance
§ for co-dominant alleles, it is not correct to use a capital &

small letter to represent them
§ a capital letter is used to represent the gene, & a superscript
to represent the allele.
C𝑅 is the allele for red flower C𝑊 is the allele for white flower
Genotype Phenotype
C𝑅 C𝑅 red
C𝑅 C𝑊 pink
C𝑊 C𝑊 white
Table 10.1: Incomplete dominance

inheritance
Figure 10.4: Incomplete dominance

in snapdragon plants. (a) Cross-
ing two pink-flowered snapdragon
plants & (b) crossing a pink-flowered
snapdragon with a white-flowered
snapdragon.
Test cross
7: test cross: a genetic cross in which § it is also called a back cross 7

an organism showing the dominant § the genotype of an F1 8 organism produced by crossing a
characteristic is crossed with a ho- homozygous dominant & homozygous recessive parent is
mozygous recessive organism; the heterozygous, but shows the dominant phenotype
phenotypes of the offspring can indi-
§ an organism displaying the recessive phenotype must have a
cate whether the original organism
homozygous recessive genotype
is homozygous or heterozygous
§ an F2 9 showing a dominant phenotype may be either
8: F1 generation: the offspring result-
homozygous or heterozygous
ing from the cross between individ-
uals with a homozygous recessive &
§ to know the genotype of such an organism, a test cross is
a homozygous dominant genotype carried out
9: F2 generation: the offspring result-
§ by crossing an organism having an unknown genotype with
ing from a cross e between two F1 a homozygous recessive organism, it is possible to determine
individuals the unknown genotype within the breeding generation
• if all the offspring are showing the dominant genotype,
the unknown parental genotype is homozygous
dominant A test cross was carried out

• a ratio of 1 dominant phenotype : 1 recessive phenotype between a brown rabbit & a
indicates that the unknown parent is heterozygous white rabbit. Five brown off-
spring & one white offspring
were produced. Use a genetic
Sex linkage diagram to show how this in-
dicates that the brown rabbit
§ in a human cell, there are two sex chromosomes must be heterozygous.
§ a woman has two X chromosomes.
§ a man has an X chromosome & a Y chromosome.
§ the X chromosome is longer than the Y chromosome.
§ most of the genes on the X chromosome are not present on
032
the Y chromosome.
§ these genes are called sex-linked genes
214
Genotype Phenotype
X𝐴 X𝐴 female with normal vision

X𝐴 X 𝑎 female with normal vision
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X𝑎 X𝑎 female with colour blindness
X𝐴 Y male with normal blindness
X𝑎 Y male with colour blindness
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Figure 10.5: Inheritance of sex-

linked traits
§ one of the genes on the X chromosome codes for the

production of a factor necessary for blood clotting, called
factor VIII.
§ there are two alleles, a dominant one that codes a for the
normal factor VIII, & a recessive one which results in the lack
of factor VIII
• we can use the symbols F & f for these two alleles
§ a person with only this recessive allele, & no dominant allele,

does not make factor VIII.
§ their blood does not clot normally, & they have haemophilia.
§ a woman has two X chromosomes, each with one copy of
this gene.
§ the woman therefore has three possible genotypes, shown
like this:
Genotype Phenotype
X𝐹 X𝐹 female with normal blood clotting

X𝐹 X 𝑓 female with normal blooding clotting
X𝑓 X𝑓 female with haemophilia
§ a man, however, has only one X chromosome, there are

therefore only two genotypes that he can have:
Genotype Phenotype
X𝐹 Y male with normal blood clotting

X𝑓 Y male with haemophilia
Figure 10.6: Inheritance of sex-

linked traits
§ sex-linked genes are shown by writing the symbol for the

allele as a superscript above the symbol for the X
chromosome.
§ there are three possible genotypes for a female, but only two
possible genotypes for a male.
§ always show the X & Y chromosomes when working with

sex-linked genes.
§ a boy cannot inherit a sex-linked gene from his father,
because he only gets a Y chromosome from his father.
• his X chromosome (which carries sex-linked genes)
comes from his mother.
10.3.2 Dihybrid crosses
§ the inheritance of two different characteristics in an organism

is called dihybrid inheritance.
032
§ in many cases these characteristics are each controlled by a
gene, consisting of a pair of alleles, inherited independently
from each other because the two genes are located on
214
different chromosomes
§ at meiosis they separate independently from other
characteristics
§ genetic diagrams can be used to show inheritance of two
733
different characteristics in an individual: this is called a
dihybrid cross
o0
oy
F. M
Mr
• for example, a breed of dog may have genes for

hair colour & leg length.
• allele A is dominant & gives brown hair
• allele a is recessive & gives black hair
• allele L is dominant & gives long legs.
• allele l is recessive & gives short legs.
• always begin by writing down all the possible
genotypes & phenotypes.
032
Genotype Phenotype
AALL brown hair, long legs

AaLL brown hair, long legs
214
aaLL black hair, long legs
AALl brown hair, long legs
AaLl brown hair, long legs
733
aaLl black hair, long legs
AAll brown hair, short legs
Aall brown hair, short legs
o0
aall black hair, short legs
• always write the two alleles of one gene together

oy
• do not mix up alleles of the two different genes

• always write the alleles in the same order.
F. M
∗ here, we have decided to write the alleles for

hair colour first, followed by the alleles for
leg length
∗ do not swap these round part-way through
Mr
• now consider the gametes that can be produced

by a dog with the genotype AaLl
• during meiosis, the chromosome with the A/a
gene and the one with the L/l gene behave entirely
independently of one another.
• at the end of meiosis, this dog will produce four
types of sperm or eggs
• half will have allele A for coat colour, and half
will have allele a
• of these, half of those with allele A will have allele
L for leg length and half will have allele l
• the same is true for those with allele a.
• so the genotypes of this dog’s gametes are:
AL Al
textbfaL al
032
Figure 10.7: Dihybrid inheritance
214
§ we would therefore expect offspring in the ratio 9 brown hair,
long legs : 3 brown hair, short legs : 3 black hair, long legs : 1
black hair, short legs.
§ Each gamete contains one allele of each gene (one of either A
733
or a, and one of either L or l).
§ the ratio 9:3:3:1 is typical of a dihybrid cross between two
heterozygotes,where the alleles of both genes show
dominance (as opposed to co-dominance).
o0
§ in tomato plants there is a gene that codes for stem colour.

This gene has two alleles:
stem colour gene
oy
A = allele forb purple stem

a = allele for green stem
• where A is dominant and a is recessive
F. M
§ a different gene, at a different locus on a different

chromosome, codes for leaf shape. Again, there are two
alleles:
leaf shape gene
D = allele for cut leaves (jagged edges)
Mr
d = allele for potato leaves (smooth edges)

• where D is dominant and d is recessive
032
214
Figure 10.8: Dihybrid inheritance
733
10.3.3 Chi squared tests
§ genetic diagrams can be used to tell the probabilities of

particular genotypes occurring in offspring
o0
§ these are just probabilities, the actual phenotypic ratios are

rarely exactly as we predicted.
§ for example, if a plant has genes for flower colour (allele Y
oy
for yellow and y for white flowers) and petal size (P for large
petals and p for small petals).
§ we cross two plants that are heterozygous for both alleles.
F. M
§ we would expect to get offspring with phenotypes:
yellow, large yellow, small white, large white, small

9 3 3 1
Mr
§ however, what we actually get are 847 offspring with these

phenotypes:

489 151 159 48
§ what we would expect to have got is:

476 159 159 53
§ the question is: are these results close enough to the expected
results to indicate that we are right in thinking that the two
genes are not linked
§ in other words, is the difference between the observed and

expected results significant?
§ a chi-squared test is used to check this
§ null hypothesis - the observed results are not significantly
different from the expected results
§ alternate hypothesis - the observed results are significantly
different from the expected results
§ if the probability of the null hypothesis being correct is
greater than or equal to 0.05, then we can accept the null
hypothesis
§ if the probability is less than 0.05 that the null hypothesis is
correct, we must reject the null hypothesis
yellow, yellow, white, white,

large small large small
observed num-
bers, O
expected num-
bers, E
O- E
(O-E)2
p𝑂 ´𝐸 q2
𝐸
§ fill in the observed numbers and the expected numbers for

each category.
§ calculate O E for each category.
§ calculate (O E)2 for each category.
p𝑂´𝐸q2
§ calculate 𝐸 for each category.
p𝑂´𝐸q2
§ add together all of the 𝐸 values, to give you Σ(O-E)2 /E
yellow, yellow, white, white,

large small large small
observed num- 489 151 159 48

bers, O
expected num- 476 159 159 53
bers, E
O- E 13 -8 0 -5
2
(O-E) 169 64 0 25
p𝑂 ´𝐸 q2
𝐸 0.36 0.40 0 0.47
§ Σp𝑂 ´ 𝐸q2 /E = 1.23, which is the 𝜒 2 value

§ now need to look this up in a probability table, to find out
what it tells us about the probability of the null hypothesis
being correct.
§ this is a part of a probability table for chi-squared values.
§ the numbers in the first column are degrees of freedom.
§ you have to choose the correct row in the table for the
number of degrees of freedom in your data.
§ in general:
degrees of freedom = number of different categories 1
§ in this case, there were four categories (the four different
phenotypes), so there are 3 degrees of freedom.
032
214
§ Look along the row for 3 degrees of freedom until you find
733
the number closest to the chi-squared value you have
calculated. This was 1.23, and all the numbers in the row are
much bigger than this. The closest is 6.25.
o0
§ Look at the probability associated with this number. It is 0.1.

This means that if the chi-squared value was 6.25, there is a
0.1 probability that the null hypothesis is correct.
oy
§ Remember that, if the probability of the null hypothesis

being correct is equal to or greater than 0.05, you can accept
it as being correct. 0.1 is much bigger than 0.05, so you can
F. M
definitely accept the null hypothesis as being correct. Indeed,

because your value of chi-squared was actually much smaller
than 6.25, we would need to go a long way further left in the
table, which would take us into probabilities even greater
than 0.1.
Mr
§ We can therefore say that the difference between the

observed results and expected results is not significant. The
differences between them are just due to random chance.
032
214
733
o0
oy
F. M
Mr
10.4 Questions
1) During research into the mechanism of DNA replica-

tion, bacteria were grown on a medium containing
nitrogen isotopes. The nitrogen isotopes used were
1heavy’ nitrogen, 15
𝑁 , & ‘light’ nitrogen, 14
𝑁 . After
growth, the bacterial DNA was isolated from the cells
and spun in a centrifuge. The DNA settled in the
centrifuge tube at a position that corresponded to its
density, indicating the proportion of the different types
of DNA present in the sample. Bacteria were grown
for many generations in a medium containing only the
‘heavy’ isotope of nitrogen 15 𝑁 . This resulted in all the
DNA molecules containing only 15 𝑁 . The result after
centrifuge is shown in the first diagram (Fig 6.1).
These bacteria were then grown in a medium contain-

ing only ‘light’ nitrogen, 14 𝑁 . After allowing time for
the DNA to replicate once, the DNA was analysed as
before. The result is shown above second diagram (Fig.
6.2).
a) Explain how this information supports the semi-
conservative hypothesis of DNA replication. [4]
The bacteria were allowed to continue to grow
in the ‘light’ nitrogen, 14
𝑁 , until the DNA had
replicated once more. The DNA was analysed as
before and the result in Fig 6.3.
10.4. QUESTIONS 151
Fig 6.4 shows simple diagrams of DNA molecules,

indicating the nitrogen content of each.
032
214
b) Select the letter from Fig 6.4 representing the bacterial
733
DNA if Fig. 6.1, Fig. 6.2 & Fig 6.3. [3]
c) The bacteria were allowed to continue to grow in the
‘light’ nitrogen, 14 𝑁 , until the DNA had replicated once
more. The DNA molecules were analysed as before.
o0
Complete the diagram to indicate the expected results

showing the composition of these DNA molecules. [2]
oy
F. M
Mr
Mr
F. M
oy
o0
733
214
032
11 Inherited change & evolution
032
This chapter contains notes on inherited change & evolution.
214 11.1 Objectives . . . . . . . 153
733
11.1.1 Variation . . . . . . . . 153
11.1 Objectives 11.2 Natural selection . . 154
11.2.1 Selection pressures &
Objectives survival . . . . . . . . 155
o0
11.2.2 Stabilising, directional

§ Natural selection & disruptive selection 155
• explain, with examples, how mutations & environment may affect pheno- 11.3 Artificial selection . . 157
type 11.3.1 Inbreeding . . . . . . 158
oy
• explain, with examples, how environmental factors act as forces of natural 11.3.2 Outbreeding . . . . . 158
selection 11.4 Questions . . . . . . . 159
• explain how natural selection may bring about evolution
F. M
§ Artificial selection
• describe one example of artificial selection
11.1.1 Variation
Mr
§ sexual reproduction produces genetic variation 1 among the 1: genetic variation: differences be-
individuals in a population tween the DNA base sequences of
§ genetic variation is caused by: individuals within a species
1. independent assortment of chromosomes, & therefore

alleles, during meiosis
2. crossing over between chromatids of homologous
chromosomes during meiosis
3. random fusion of gametes, & random mating between
organisms within a species
4. mutation
§ the first three these processes reshuffle existing alleles in the
population
§ offspring have combinations of alleles which differ from

those of their parents & from each other
2: phenotypic variation: differences § this genetic variation produces phenotypic variation 2
between the observable character- § mutation, however, does not reshuffle alleles that are already
istics of individuals within a species present
§ mutations produce completely new alleles
§ the environment also affects phenotype
§ differences between the phenotypes of individuals belonging
to the same species are known as variation
§ variation can be continuous or discontinuous
3: continuous variation: differences 1. continuous 3 variation occurs when a feature can have
032
between individuals of a species in any value between two extremes, such as height & mass
which each one can lie at any point in humans
in the range between the highest &
• it is affected by genes & the environment
lowest values
• a different alleles at a single gene locus have small
214
effects on the phenotype
• different genes have the same, often additive, effect
on the phenotype
• a large number of genes may have a combined effect
733
on a particular phenotypic trait; these genes are
4: polygenes: a number of different known as polygenes 4
genes at different loci that all con- 2. discontinuous 5 variation occurs when a feature has only
o0
tribute g to a particular aspect of

a few distinct categories, such as blood groups in
phenotype
humans
5: discontinuous variation: differ-
• it is affected by genes & the environment has not
ences between individuals of a
oy
species in which each one belongs

effect
to one of a small number of distinct • different alleles at a single gene locus have large
categories, with no intermediates effects on the phenotype
F. M
§ generally, continuous variation is caused when the effects of

many different genes act together to influence a characteristic
§ the environment may also have an effect in continuos
variation
§ discontinuous variation is caused by one or a few genes that
Mr
control the characteristic, with little or no influence from the

environment
11.2 Natural selection
§ process by which organisms which appear physically,

physiologically & behaviourally better to the environment
survive & reproduce
• these organisms pass on their successful characteristics
to the next generation
§ organisms not so well adapted either fail to reproduce or die
11.2. NATURAL SELECTION 155
• these organisms fail to pass on their characteristics to the

next generation
§ selection depends on phenotypic variation
§ selection is part of the mechanism by which a species adapts
to its environment
§ all organisms have the reproductive potential to increase
their populations
§ as a population of organisms increases, various environmental
factors come into play to keep down the population size &
these act as selection pressures 6 6: selection pressure: - a factor that
§ these factors may be biotic factors, (predation, competition for gives a greater chance of surviving
032
food, or infection by pathogens) or they may be abiotic factors to some members of the population
(water supply or nutrient levels in the soil) than others.
§ the number of young produced is far greater than the

number which will survive to adulthood
214
§ many young die before reaching reproductive age
11.2.1 Selection pressures & survival

733
§ variation within a population of means that some will have
features which give them advantage in the ‘struggle for
existence’
o0
§ selection pressure increase the chances of some alleles being

passed on to the next generation & decrease the chances of
others
oy
§ the effect of selection pressures on the frequency of alleles in

a population is called natural selection 7 7: natural selection: is the increased
F. M
§ natural selection increases the frequency of alleles conferring chance of survival & reproduction
an advantage, & reduces the frequency of alleles conferring a of organisms with particular phe-
disadvantage. notypes, because they are better
adapted to their environment than
§ over time, it ensures that the individuals in a population
those with other phenotypes.
have features that enable them to survive & reproduce in
their environment
Mr
11.2.2 Stabilising, directional & disruptive selection
Stabilising selection
§ stabilising selection 8 occurs when the environment is fairly 8: stabilising selection: natural selec-
stable & organisms in a population are already well adapted tion that tends to keep frequencies
to their environment relatively constant over many gener-
§ a population remains stable for a particular character or trait ations
if selection acts on variation & removes the extremes

§ e.g a study of human birth weight in 1973 showed that there
is higher mortality in very small & very large babies
Figure 11.1: Stabilising selection
032
§ this means that the birth weight remains fairly stable with
only a narrow range around the mean birth mass
§ this is an example of stabilising selection
214
§ if a new, extreme phenotype (i.e. one that lies far from the
mean) arises it will have no selective advantage & so will not
be selected
Figure 11.2: Stabilising selection in
733
birth mass in human babies. The red
line represents mortality rate.
Directional selection
§ in a changing environment individuals with features more

o0
suited to the new environment will be selected

§ these will be more likely to survive long enough to breed &
have offspring
oy
§ this gives them a competitive advantage & the features (and

the alleles producing them) have a greater chance of passing
to future generations
F. M
9: directional selection: selection that § this is directional selection, 9 where an increasing proportion
natural causes a gradual change in of individuals shows the advantageous feature & fewer show
allele frequency over many genera- any of the other features
tions § as a result, the population changes
Mr
Figure 11.3: Directional selection
Disruptive selection
11.3. ARTIFICIAL SELECTION 157
§ disruptive selection, can occur when conditions favour both

extremes of a population
§ this type of selection maintains different phenotypes
(polymorphism) 10 in a population 10: polymorphism: the continued ex-
§ it occurs when an environmental factor, such as temperature istence of two or more different phe-
takes two or more distinct forms notypes in a species
032
214
Figure 11.4: Disruptive selection
733
11.3 Artificial selection
o0
§ artificial selection 11 is a process in which humans determine 11: artificial selection: the selection by
which individuals survive & reproduce humans of organisms with desired
traits to survive & reproduce; also
1. the population that is to be used for artificial selection
oy
known as selective breeding

must b show some variation. For example, some
individuals in a variety of wheat may have resistance to
a disease, while others are killed by it.
F. M
2. the breeder selects an individual that has the features

features that she wants future generations to have. In
this case, she would select a plant that has better
resistance to the disease than other individuals.
3. She then selects another parent plant. This could be
Mr
from the same variety & also have good resistance to

disease. However, in some cases, the breeder might
select a parent from a different variety that shows
another beneficial characteristic, such as high yield, if
she wants to produce a new variety with a good
combination of disease resistance & high yield.
4. the two chosen parents are then bred together.
5. the resulting offspring are grown to adulthood and
tested
6. this process continues for many generations, each time
selecting the ‘best’ individuals for breeding, until all
individuals show the desired characteristic or
characteristics
§ in artificial selection, breeders are exerting a directional

selection pressure
§ this leads to changes in allele & genotype frequencies within
the population
§ this is an evolutionary mechanism which gives rise to new
breeds, strains, varieties, races & subspecies
11.3.1 Inbreeding
12: inbreeding: breeding o between § inbreeding 12 involves selective reproduction between closely
organisms with similar genotypes, related organisms
or that are closely related § this is done in order to propagate particularly desirable
characteristics
§ this usually achieves genetic uniformity
§ it was used by livestock breeders to produce cattle, pigs,
poultry & sheep with high yields of milk, meat, eggs & wool
respectively
§ it was also used to produce donkeys with high endurance &
speed
§ however it is nolonger widely practised due to the following
reasons
1. prolonged inbreeding can lead to a reduction in fertility
2. it reduces the variability of the genome by increasing the
number of homozygous genotypes at the expense of
heterozygous genotypes
3. this results in inbreeding depression, in plants it results in
weak plants with low yields
11.3.2 Outbreeding
13: outbreeding: breeding between in- § outbreeding 13 usually useful in plant breeding, but is being
dividuals that are not closely related used in the commercial production of meat, wool, eggs
§ it involves crossing individuals from genetically distinct
populations
§ the progeny are known as hybrids
§ hybrids have phenotypes showing characteristics superior to
either of the parental stock
14: hybrid vigour: an increased ability • this is called hybrid vigour 14 or heterosis
to survive & grow well, as a result of § increased vigour results from the increased heterozygosity
outbreeding & therefore increased
which arises from gene mixing
heterozygosity
§ increased vigour may also result from some form of
interaction between particular combinations of alleles in the
heterozygote
§ if F1 phenotypes are continually inbred, vigour will decrease
due to an increase in the proportion of homozygotes
11.4. QUESTIONS 159
§ selective hybridisation can induce polyploidy, which can

lead to the production of new species
Differences between artificial & natural selection
§ Artificial selection is similar to natural selection, in that

individuals with particular characteristics are more likely to
breed than others.
§ However, in artificial selection, individuals without these
characteristics will not breed at all, whereas in natural
selection there is still a chance that they might breed.
032
§ Artificial selection may therefore produce bigger changes in
fewer generations than natural selection normally does.
§ The breeders do not need to know anything about the genes
or alleles that confer the characteristics they want their
214
plants to have; they just choose the plants with those
characteristics & hope that the appropriate alleles will be
passed on to the next generation.
§ Artificial selection usually requires many generations of
733
selection before the desired result is obtained.
o0
11.4 Questions
oy
F. M
Mr
1) Resistance to the poison warfarin is now extremely

common in rats. Warfarin inhibits an enzyme in the
liver that is necessary for the recycling of vitamin K.
Vitamin K is involved in the production of substances
required for blood clotting. There are two alleles of the
gene that codes for this enzyme. Resistant rats have the
allele R𝑅 ; rats susceptible to warfarin have the genotype
𝑅𝑆 𝑅𝑆 .
• Rats susceptible to warfarin die of internal bleed-
032
ing
• Homozygous resistant rats do not suffer internal
bleeding if their diets provides more that 70 𝜇g
214
of vitamin K per kg body mass per day
• heterozygous rats are resistant to warfarin if their
diet provides about 10 𝜇g of vitamin K per kg
body mass per day
733
a) A population of rats was studied in an area where
warfarin was used. The dietary intake of rats was
about 15 𝜇g of vitamin K per kg body mass per
day
o0
Complete the table below to indicate whether

rats of the three genotypes have a high or a low
chance of surviving to maturity in this population.
oy
Explain each of your answers. [3]
genotype chance of explanation

F. M
surviving
to maturity
𝑅𝑅 𝑅𝑅
𝑅𝑅 𝑅𝑆
𝑅𝑆 𝑅𝑆
Mr
b) i) State how the allele for warfarin resistance

originated. [1]
ii) Explain how the allele spread throughout the
population. [5]
c) State why this is an example of natural selection.
[1]
d) Explain what is likely to happen to the frequen-
cies of the two alleles (𝑅 𝑅 & 𝑅 𝑆 ) within the rat
population over a period of time if warfarin use
is discontinued. [2]
Mr
F. M
oy
o0
Upper Six
733
214
032
Mr
F. M
oy
o0
733
214
032
Mr
F. M
oy
o0
733 Appendix
214
032
Mr
F. M
oy
o0
733
214
032
Alphabetical Index
adenine, 4 10 RER, 18
aminoacyl- DNA-helicase, RNA, 3
tRNA, 10 RNA poly-
18 merase,
nucleolus, 8
anticidon, 8 14
nucleoside, 4
anticodon, 18
nucleotide, 4 semi-
cytosine, 4 conservative,
phosphodiester,
10
dinucleotide, 5, 14
5 polynucleotide, thymine, 4
DNA, 3 5 transcription,
DNA ligase, 11 polyribosome, 7
DNA poly- 17
merase, polysome, 17 uracil, 4

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A’ Level Biology Notes

A compilation of my A’ level notes

. M Mpopoma High School

– To Goodwill & Reaboka Moyo

1 Cell Structure and Function 3

1.4.7 Golgi apparatus . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 12

1.5.1 Prokaryotic cells . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 18

2 Biological Molecules and Water 25

3.3.1 Factors affecting rate of activity . . . . . . . . . . . . . . . . . . . . 47

4 ATP & Photosynthesis 55

4.3.3 Absorption & action spectra . . . . . . . . . . . . . . . . . . . . . . 60

6 Sexual Reproduction in plants 77

7.4 Oxygen transport . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 85

7.4.3 Oxygen transport . . . . . . . . . . . . . . . . . . . . . . . . . . . . 87

7.4.5 Dissociation curve . . . . . . . . . . . . . . . . . . . . . . . . . . . . 89

8 Cell and nuclear division 99

10.2.1 Genes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 135

10.3.1 Monohybrid crosses . . . . . . . . . . . . . . . . . . . . . . . . . . . 136

10.3.3 Chi squared tests . . . . . . . . . . . . . . . . . . . . . . . . . . . . 146

11 Inherited change & evolution 153

11.2 Natural selection . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 154

Upper Six 161

Alphabetical Index 165

1.1 Optical microscope . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4

2.18 Formation of triglycerides . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 36

3.1 Difference between a catalysed & uncatalysed reaction . . . . . . . . . . . . . 46

5.4 The Kreb cycle . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 72

6.1 Development of pollen grain . . . . . . . . . . . . . . . . . . . . . . . . . . . . 78

6.3 Development of ovule . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 79

7.1 A comparison of blood vessels . . . . . . . . . . . . . . . . . . . . . . . . . . . 84

7.4 Structure of haemoglobin . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 86

9.1 Pentose sugar . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 118

9.6 Dinucleotide . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 119

9.8 Structure of DNA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 120

9.14 DNA replication . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 126

10.1 Different allele combinations . . . . . . . . . . . . . . . . . . . . . . . . . . . . 136

11.1 Stabilising selection . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 156

1.1 Differences between light & electron microscope . . . . . . . . . . . . . . . . . 5

5.1 Complete breakdown of glucose . . . . . . . . . . . . . . . . . . . . . . . . . . 73

5.2 ATP used & generated . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 74

8.1 Differences between mitosis in plants & animals cells. . . . . . . . . . . . . . . 105

9.1 Differences between DNA and RNA . . . . . . . . . . . . . . . . . . . . . . . . 122

10.1 Incomplete dominance inheritance . . . . . . . . . . . . . . . . . . . . . . . . . 139

draw and determine linear dimensions of specimens

1.4 Organelles & func-

§ Organelles and their functions 1.4.3 Endoplasmic reticulum 10

1.4.7 Golgi apparatus . . . . 12

Figure 1.1: Optical microscope

§ the total magnification is calculated by multiplying the num-

§ magnification is the number of times a specimen is enlarged

§ they can produce images with a magnification of up to x 500

§ there are two types (TEMs) & (SEMs).

Differences between light & electron microscope

1.3 Plant and Animal Cells

1.3.2 Animal cells

1.4 Organelles & functions

Diagram Structure Function

nuclear pores § genes control