Daniel Ramcharan

Biology Cape Unit 1 Module 1

THIS MODULE CONTAINS FOUR TOPICS:

1. ASPECTS OF BIOCHEMISTRY
2. CELL STRUCTURE
3. MEMBRANE STRUCTURE AND FUNCTION
4. ENZYMES
 Daniel Ramchara
TOPIC 1
BIOCHEMISTRY
Water in plants :-
Transpiration in Plants:
• Water is crucial in the process of transpiration.
• Transpiration is the loss of water vapour from a plant to the outside atmosphere.
• Occurs mainly through the stomata of leaves.

Transport of Solutes and Photosynthesis Products:

• Achieved via the phloem.
• Facilitated by water.
• The phloem is specialised for the transport of organic and inorganic materials within plants.
Role of Xylem:
• Conducts water and minerals upwards from the roots to all parts of the plant.

Water in animals:-

Circulatory System of Mammals:

• The heart pumps blood throughout the body.
• Blood is approximately 90% water.
• Blood transports nutrients and gases to organs.
• Blood carries metabolic wastes away from organs.

Excretion of Nitrogenous Wastes:

h
• Water is important in the excretion of nitrogenous wastes in urine.

H
Properties of water

1 Cohesion and Surface Tension:

Dynamic Structure of Liquid Water:
• Water molecules move about and continually break and re-establish hydrogen bonds.
High Cohesive Strength of Water:
• Presence of hydrogen bonds explains water’s high cohesive strength.
• Permits narrow columns of water in the xylem of plants to reach the top of tall trees (e.g., cabbage palms,
Casuarina equisetifolia).
• Water evaporates from leaf cells and diffuses to the atmosphere.
• Transpiration causes the entire column of water to move upwards due to the pull of evaporating water molecules.
• Water vapour diffuses from leaf intercellular spaces during transpiration.
• Cohesive strength and evaporation cause a flow of water from the roots up through the plant.
High Surface Tension:
• Surface between liquid water and air is relatively difficult to puncture.
• A lot of energy is needed to force hydrogen-bonded water molecules apart.
• Allows a container to be filled slightly above its rim without overflowing.
• Example: Filling a clean glass with water above its rim.
• Permits very small animals to walk on water surfaces.
 2 • Freezing and Crystalline Structure:
• When water freezes, it forms a crystalline structure with water molecules arranged in a hexagonal pattern.
• Each water molecule in ice is hydrogen-bonded to four other molecules in a three-dimensional lattice.
• Density of Water and Ice:
• Water molecules in ice are less closely packed than in liquid water, making ice less dense and allowing it to
float.
• Water becomes denser as it cools down to 4°C, but between 4°C and 0°C, it becomes less dense.
• Maximum density of water occurs at 4°C.
• Biological Impact:
• In ponds and lakes, denser water at 4°C sinks, while less dense water at temperatures below 4°C stays at
the top and freezes.
• The floating ice forms an insulating layer, helping aquatic life survive in the liquid water beneath.

3. • Heat of fusion and heat of vaporisation

Heat of Fusion:
• Melting ice requires a large amount of heat energy, known as the latent heat of fusion.
• Melting one mole of water molecules from solid to liquid at 0°C requires 6.0 kJ of energy.
• The high energy requirement is due to the large number of hydrogen bonds that must be broken to change
ice into liquid water.
• During freezing (conversion of liquid water to solid), the same amount of heat energy is released to the
surroundings.

• Heat of Vaporisation:
• Water has a high heat of vaporisation, the amount of heat required to convert liquid water into gaseous water.
• Evaporation occurs as liquid water absorbs heat from the environment, converting it to vapour.
• The absorbed heat energy breaks the hydrogen bonds, allowing water molecules to move freely and become
gas.
• Evaporation has a cooling effect, as seen in the cooling of our bodies when perspiration evaporates, using up
body heat.

• Water as a Temperature Moderator:

• Water is effective at moderating temperature changes due to the high energy required to change its physical
state (gas, liquid, solid).
~

4 • Heat capacity of water

High Specific Heat Capacity of Water:

• Liquid water has a high specific heat capacity.
• Specific heat capacity is the amount of heat energy required to raise the temperature of 1 kg of water by 1°C.
• Unit of specific heat capacity: Jkg⁻¹ °C⁻¹ (joules per kilogram per degree Celsius).

• Temperature Regulation:
• The high specific heat capacity of water allows bodies of water like oceans and rivers to maintain temperatures
within a small range throughout the year.
• Coastal and island temperatures are moderated by the oceans, resulting in less temperature variation compared to
land.
• Sea water temperature changes less than land temperature when exposed to sunlight, making the water feel cool
even on sunny days.

Effects of temperature on sea water and life within it :

• Corals and Sea Water Temperature:

• Increased sea water temperature due to climate change negatively affects corals by driving out dissolved oxygen.
• Corals are cold-blooded, so their metabolism increases with temperature, leading to higher energy and oxygen
demands.
• A temperature rise of 1–2°C stresses corals, especially at night, and can cause coral bleaching.
• Coral Bleaching:
• Corals bleach when exposed to higher temperatures, expelling zooxanthellae and revealing their white skeleton.
• Zooxanthellae are algae that live symbiotically with corals, aiding in photosynthesis.
Solvent properties of water

Aqueous Solutions:
• Many metabolic reactions occur in an aqueous solution, where water serves as the solvent.
• A solution is a uniform mixture consisting of a solute (present in a lesser amount) and a solvent (present in
a greater amount, usually water).
• Aqueous solutions are crucial mediums for biochemical reactions, such as enzyme activity within living
organisms.

• Water as a Solvent:
• Water is a highly effective solvent for polar or charged molecules due to its polar nature.
• Water molecules are electrically polar, with partial positive and negative charges that allow them to
separate ionic substances, like sodium chloride (NaCl), into Na+ and Cl– ions.
• When NaCl is added to water, water molecules cluster around the individual ions, separating them from
each other. The negative regions of water molecules align with Na+ ions, while the positive regions align with Cl– ions.

• Solubility of Polar and Nonpolar Molecules:

• Polar molecules, such as sucrose and glucose, dissolve easily in water and are described as hydrophilic
(water-loving).
• Non-polar molecules, such as lipids and fats, do not dissolve in water because they cannot form hydrogen
bonds with water molecules.
• Non-polar molecules tend to cluster together in water, forming hydrophobic interactions. For example,
when oil is added to water, it coalesces on the surface, and even if stirred vigorously, it eventually separates out.

• Impact on Larger Molecules:

• The solubility of large protein or carbohydrate molecules in water depends on the distribution of
hydrophobic (water-hating) and hydrophilic (water-loving) regions on the molecule.
• Hydrophobic regions repel water and tend to cluster together, while hydrophilic regions attract water and
tend to dissolve easily.

Carbohydrates

• Carbohydrates are the most abundant organic molecules in nature.

• They serve as the primary energy-storage molecules in most living organisms.
• Carbohydrates contain carbon-carbon (C–C) and carbon-oxygen (C–O) bonds.
• When carbohydrates are used as fuel:
• Carbon is converted to carbon dioxide (C=O bonds).
• Hydrogen is converted to water (O–H bonds).
• The energy released from the formation of C=O and O–H bonds is greater than the
energy required to split the original C–C and C–O bonds.
• This released energy is used by body tissues to perform functions like walking,
running, talking, and digestion.
• Carbohydrates also form structural components of cells.
• Plant cell walls consist of cellulose, a carbohydrate, embedded in a matrix of other
carbohydrates and protein.
 • Carbohydrates are formed from small molecules called sugars. How it's form
• Carbohydrates are classified based on the number of sugar units they contain:
• Monosaccharides: Consist of a single sugar molecule (e.g., glucose, fructose).
• Disaccharides: Contain two sugar molecules covalently linked (e.g., sucrose, lactose).
• Polysaccharides: Contain many sugar units covalently linked together; they are macromolecules
(large molecules).
• All carbohydrates have a 2:1 ratio of hydrogen (H) to oxygen (O).
• Polymerisation: Process where monomers (individual small units) are covalently linked to form a
polymer.
• Polymers are macromolecules.
• Amino acids: Individual monomers that link together to form proteins, which are
macromolecules.
• Molecular formula: Indicates the number of atoms of each kind in a molecule.
• Structural formula: Shows how atoms are bonded to each other.
• – represents a single covalent bond, and = represents a double covalent bond.

Condensation and Hydrolysis Reactions

• Condensation reactions: loss of He d
• Occur when two monosaccharides join to form a disaccharide.
• A molecule of water is lost, and a new bond is formed.
• To synthesize a polysaccharide, many condensation reactions are needed to join.
monosaccharides together.
• Condensation reactions require an input of energy.
• Hydrolysis: addition of He

• Occurs when a disaccharide is split into its monosaccharide units.

• A molecule of water is added during the process.
• Hydrolysis is an energy-yielding process.
• Hydrolytic reactions are important in energy transfers within cells.
 Glycosidic Linkages

• Glycosidic Linkages:
• Formed by condensation reactions.
• Covalent bonds between monosaccharides.
• Used to create disaccharides or polysaccharides.
• Glucose:
• Molecular formula: C₆H₁₂O₆.
• Exists in two forms:
• Straight chain.
• Ring structure.
• Ring Structure of Glucose:
• Two types:
• * Alpha-glucose (α-glucose):
• Has specific placement of –H and –OH on the first carbon.
• A Beta-glucose (β-glucose):
• Differs from α-glucose in the placement of –H and –OH on the first carbon.
• Glycosidic Bond Formation:
• When glucose molecules form glycosidic linkages:
• The bond is either α-linked or β-linked, depending on whether the glucose at carbon 1 is in
the α or β form.
• Difference Between α and β Glucose:
• Only differ in the spatial arrangement of atoms.
• Can interconvert or change between forms in water.
• Exist in equilibrium in water.
• Anomeric Carbon:
• The carbon in glucose (or other sugars) where the hydroxyl group can be in either the α or
β form.

6 o
CHzOlt
⑧
H2C
Iti It OH

I Ho"C H
Y
Ot It
OH H " Oh

H03H 2

OH
HS-oH
·
<H2OH

↑ of
as Glucose
"Ho
O
Bramoe
 • Reducing Sugars:
• Sugars that, in solution, contain an aldehyde or ketone group.
• Functional Groups:
• Aldehyde group: A type of chemical functional group.
• E Ketone group: Another specific type of chemical functional group.
• Examples of Reducing Sugars:
• Glucose
• Fructose
structural isoners
• Hexoses:
• Glucose: A six-carbon sugar (C₆H₁₂O₆), classified as a hexose.
• Produced by plants via photosynthesis.
• Used by animals as an energy source.
• Other common hexoses (C₆H₁₂O₆):
•
•
Fructose
Mannose 7
• Galactose
• These hexoses are structural isomers of glucose, meaning:
• They have the same molecular formula but differ in how their atoms are arranged.

e •
•
•
Isomers:
Compounds with the same molecular formula but different structural arrangements.
Chemical Properties of Sugars:
• Hydroxyl groups (–OH) and carbonyl groups (>C=O) are hydrophilic.
• This allows monosaccharides and many carbohydrates to dissolve in water.

Pentoses:

• Pentoses: Five-carbon sugars. S

• Two important biological pentoses:

• Ribose: Found in RNA. Y
I

• Deoxyribose: Found in DNA.

• Both form part of the nucleic acid backbones (RNA and DNA). 2

• Structure of Pentoses:
3

• Pentoses form a five-sided ring structure.

• Functions:
• Ribose:
• Found in RNA.
• Also a component of adenosine triphosphate (ATP).
• Deoxyribose:
• Found in DNA.
 Importance of glucose, sucrose, starch,
glycogen and cellulose

Glucose:

• Sugar Unit: Monosaccharide (C₆H₁₂O₆).

• Overall Shape: Can exist as a straight chain or in a ring form.
• Solubility: Highly soluble in water.
• Glycosidic Bond: Forms α or β glycosidic bonds depending on the type of glucose.
• H Bonds: Can form hydrogen bonds due to its hydroxyl groups.
• Location: Found in all living organisms; transported in blood.

&
• Importance:
• Primary energy source for cells.
• Used to create polysaccharides like starch, cellulose, and glycogen.
• Essential for brain cell function.
• Involved in photosynthesis in plants and energy metabolism in animals.
• Uncontrolled glucose levels in blood can lead to diabetes.

Sucrose:

• Sugar Unit: Disaccharide (glucose + fructose).

• Overall Shape: Composed of one glucose and one fructose molecule.
• Solubility: Highly soluble in water.
• Glycosidic Bond: 1,2 glycosidic linkage between glucose and fructose.
• H Bonds: Limited hydrogen bonding as a disaccharide.
• Location: Commonly found in plants (e.g., sugar cane); used in transport of sugars in plants.

&
• Importance:
• Non-reducing sugar (no free anomeric hydroxyl group).
• Chemically unreactive and stable, making it ideal for sugar transport in plants. more
complex than
• Common table sugar; extracted from sugar cane. glucose and energy-efficient
more

Starch:

• Sugar Unit: Polymer of α-glucose.

• Overall Shape: Forms amylose (linear) and amylopectin (branched) structures.
• Solubility: Amylose is water-soluble, while amylopectin is not.
• Glycosidic Bond:
•
• *
Amylose: α-1,4 glycosidic linkages.
Amylopectin: α-1,4 and α-1,6 glycosidic linkages (branching every 24-30 glucose monomers).
• H Bonds: Hydrogen bonds stabilize the helical structure of amylose and cross-linkages in
amylopectin.
• Location: Found in plant storage cells (e.g., tubers like yams, potatoes).
• Importance:
•
•
•
S
Primary storage polysaccharide in plants.
Plants break it down for energy during growth and development.
Its compact structure allows for long-term energy storage.

Glycogen:

• Sugar Unit: Polymer of α-glucose.

• Overall Shape: Highly branched structure.
• Solubility: Insoluble in water.
• Glycosidic Bond:
•
•
•
[ α-1,4 glycosidic bonds along the chain.
α-1,6 glycosidic bonds at branch points (every 8-12 glucose units).
H Bonds: Hydrogen bonds provide stability in the branched structure.
• Location: Stored in liver and muscle cells in animals.
• Importance:

I
• Main energy storage molecule in animals, fungi, and some prokaryotes.
• Compact and dense, allowing for efficient storage of glucose.
• Readily hydrolyzed to release glucose for energy.
• Helps regulate osmotic pressure by reducing the number of dissolved glucose molecules.
 Cellulose:

• Sugar Unit: Polymer of β-glucose.

• Overall Shape: Long, unbranched chains forming microfibrils.
• Solubility: Insoluble in water.
• Glycosidic Bond: β-1,4 glycosidic linkages.
• H Bonds: Extensive hydrogen bonding between parallel chains creates strong cross-
linkages.
• Location: Found in plant cell walls.

E
• Importance:
• Provides structural support to plant cells, making cell walls semi-rigid.
• Indigestible by humans, contributing to dietary fiber (roughage).
• Digested by certain animals (e.g., cows, termites) with the help of microorganisms in their
gut.
• Forms microfibrils that strengthen plant cell walls.

Pectins:

• Sugar Unit: Polymers of α-galacturonic acid (a derivative of glucose).

• Location: Found in the middle lamella between plant cells.
• Importance:
• Acts as a gelling agent in fruits like guavas, aiding in the setting of jams and jellies.

structure of sucrose

CHaOlt
CH-8 is removed
H o H

O
·

CH20H

B-glo
out
H a
olf
o If of
H OH

alpha-glucose OH

beta-erose
 LIPIDS AND TRIGLYCERIDES
Chemical Structure and Functions of Lipids:

• Chemical Structure of Lipids:

• Composed of carbon, hydrogen, and oxygen atoms.
• Contain many non-polar covalent bonds, making them hydrophobic (water-insoluble).
• Lipids are insoluble in water because water is polar and lipids are non-polar.
• van der Waals forces of lipids:
• Weak but additive interactions between electron clouds of non-polar molecules.
• These forces hold lipid molecules together when they are close, maintaining their liquid or
solid state.
• Not macromolecules: Lipids are not formed by polymerization of monomers, even though
some are very large.
• Functions of Lipids:
• Energy Storage:
• Fats and oils are used by organisms to store energy.
• Plants store energy as oils, especially in seeds and fruits (e.g., peanut oil, corn oil, olive oil,
coconut oil).
• Animals convert excess sugars into fat for long-term storage.
• Fats and oils have more energy-rich carbon-hydrogen bonds than carbohydrates, thus storing
more energy.
• Fat: ~2,151 joules/gram
8 • Carbohydrate: ~956 joules/gram
• Protein: ~717 joules/gram
⑳ •
•
Insulation:
Lipids form part of the myelin sheaths on nerve cells, providing electrical insulation.

-
• Water Repellence:
• Lipids create a layer of fat or oil on skin, fur, and feathers, helping to repel water.
• Waxes:
• Form protective barrier layers, reducing water loss from plant surfaces.
• Example: Wax on sugar cane stems appears as white translucent flakes.

Triglycerides:
• Both fats and oils consist of three fatty acid molecules covalently bonded to one glycerol
molecule.
• The bonds are formed via condensation reactions, which remove a molecule of water.
• Fats and oils are also referred to as triglycerides.
• Fatty Acid Chain Properties:
• The length of the fatty acid chains affects the physical properties, such as the melting point.
• Saturation or unsaturation of fatty acids impacts their physical characteristics:
• Saturated fatty acids: Contain no double bonds between carbon atoms (all single bonds).
• Unsaturated fatty acids: Have one or more double bonds (C=C) or triple bonds (C≡C) between
carbon atoms.
• Effects of Double Bonds in Fatty Acids:
• Unsaturated fats have double bonds, causing kinks in the hydrocarbon chain, which prevent
close packing.
• Polyunsaturated fats: Have multiple kinks in the chain, leading to fewer van der Waals’ bonds
between chains.
• These kinks result in lower melting points for unsaturated fats, which are typically liquid at room
temperature.
• Saturated fats (e.g., butter, lard) have no kinks and can pack closely, so they are usually solid at
room temperature.
 • Adipose Tissue:
• Adipose tissue is a type of loose connective tissue containing adipose cells that synthesize and store
lipid droplets.
• Functions of adipose tissue:
adipocytes
• Energy storage: Provides a major source of stored energy for animals.
• Cushions organs: Provides physical protection to internal organs.
• Thermal insulation: Forms layers under the skin that reduce heat loss and act as insulation.
• Blubber: A thick fat layer found in marine mammals (e.g., whales, sea otters) that reduces heat loss
in water.
• Energy Storage and Obesity:
• When humans consume more calories than needed, excess energy is stored as fat droplets in cells.
• Excess fat storage can be used as an energy source when food intake is reduced.
• Obesity: A medical condition where the body stores excessive amounts of fat, posing health risks.
• Causes of obesity include the consumption of excess dietary calories.
• Obesity management typically involves calorie reduction and physical exercise.

condensation
Hydrolysis 3H20

3H20

ester linkage

H2C
insoluble in water and are HYDROPHOBIC
HC

H2C

Glycerol Fatty acid • Fats are broken down by the enzyme lipase
(secreted by the pancreas).
• The breakdown of fats results in the formation
of fatty acids and glycerol.
• Fatty acids are classified as either saturated
or unsaturated.
 Phospholipids

Chemical Structure and Function of Phospholipids:

• Structural Role: Phospholipids are key components of cellular membranes.

• Composition:
• Composed of three fatty acid molecules attached to a glycerol molecule.
• In phospholipids, the third carbon of the glycerol is attached to a phosphate group.
• The phosphate group is negatively charged and attached to an oppositely charged group.
• Non-polar Tails:
• The two fatty acid molecules form non-polar hydrocarbon chains.
• These tails are hydrophobic (insoluble in water).
• Polar Head:
• Contains the phosphate group.
• The R group attached to the phosphate is hydrophilic; in the simplest phospholipid, this R
group is a hydrogen atom.
• Interaction with Water:
• In water, phospholipids form a thin film or layer along the surface.
• The hydrophilic polar heads are submerged in water, while the hydrophobic tails protrude
above the surface.
• Bilayer Formation:
• When surrounded by water (like in cells), phospholipids align in double layers (bilayers).
• In the bilayer: ↑

• Polar phosphate heads face outward toward the water.

• Fatty acid tails face inward toward each other.
• Micelle Formation:
• Phospholipids can form a spherical structure called a micelle when placed in water.

Without the
phospholipid bilayer structure cells would Not
be able to
-

keep their organelles

together.
 PROTEINS AND AMINO ACIDS
Functions of Proteins:

• Structural support: Form important components of cells and tissues.

• Enzyme catalysis: Act as enzymes to speed up chemical reactions.
• Transport: Involved in the transport of molecules (e.g., hemoglobin transports oxygen).
• Defense: Play roles in immune response (e.g., antibodies).
• Movement: Involved in muscle contraction and other cellular movements.

Protein Structure:

• Proteins are polymers of amino acids arranged in a linear sequence.

• Amino acids are joined by peptide bonds (linkages between amino acids formed in condensation reactions).

Amino Acids:

• Structure:
• An amino acid contains:
• An amino group (–NH2).
• A carboxylic group (–COOH).
• A central carbon atom bonded to a hydrogen atom.
• An R group (side chain) that varies among amino acids.
• There are 20 common amino acids used in proteins, with different R groups.
• Ionization:
• In solution, the amino group ionises to –NH3⁺, and the carboxyl group ionises to –COO⁻.
• Ionisation depends on pH, and there is a specific pH where the overall charge of the amino acid is zero.
• Amino Acid Diversity:
• Amino acids can be polar, non-polar, or charged.
• This influences the hydrophobic or hydrophilic nature of the protein.

Peptide Bonds and Polypeptides:

• Peptide bond: A covalent bond between the amino group of one amino acid and the carboxyl group of
another amino acid, with the loss of a water molecule.

How
• A sequence of amino acids linked by peptide bonds forms a polypeptide.
• The start of the chain (first amino acid) is the N-terminus (amino group). are polypeptida
• The end of the chain (last amino acid) is the C-terminus (carboxyl group).

Molecular Mass of Proteins:

• Proteins have a relative molecular mass ranging from 10,000 to 1,000,000,000.

• Compared to smaller molecules:
• Glucose has a relative molecular mass of 180.
• Water has a relative molecular mass of 18.
HHO
HNC C
·

Oh

amino Side in
Carboxyl
group group
 Amino acids can bond with each other during
condensation reactions.
The linkages formed are
very strong covalent bonds called PEPTIDE
BONDS.
When this occurs, a H atom joins with an –OH
to form a water molecule.

Protein synthesis occurs in the RIBOSOMES of the cells.

· As previously said, condensation reactions occur when amino acids are bonded,
which produce water molecules.

When many of these amino acids are linked by peptide bonds, the chain itself is called a
POLYPEPTIDE.

⑧ These polypeptide chains eventually come together to form structures of

protein.

H
H H

CC
OH
B R
Single amino acid
single amino acid

condensation
H20
HH # I O

HNC < NC CON

R B
peptide
- bond

Dipeptide molecule

By the of break
use

hydrolysis to molecule
the dipeptide
 How acids there
There are 20 amino acids.
amino are

many
They may be hydrophilic or hydrophobic.
Only the ones with side chains (‘R’
groups) that contain ring structures are hydrophobic. Here are a few examples of amino
acids.
- Serine – Used in the synthesis of components in the brain cell membranes and neurones.
- Leucine – Involved in increasing lean muscle mass.
- Valine – High levels are associated with insulin resistance and diabetes.
- Tryptophan – Converts to serotonin, which affects mood and sleep
- Aspartic acid – Contributes to the formation of urea.

Structure of proteins

• Primary Structure:
• Linear sequence of amino acids in a protein.
• Composed of a repeating sequence of –N–C–C (nitrogen-carbon-carbon).
• Determines structural features and biological function.
• Each protein has a unique amino acid sequence.
• A small variation in sequence can alter or destroy protein function.
• Secondary Structure:
• Folding of the polypeptide chain due to interactions among amino acids.
• Two main types: α-helix and β-pleated sheet.
• α-helix:
• Held by hydrogen bonds between the double-bonded oxygen in one amino acid and hydrogen in the
amino group of another (4 amino acids away).
• R groups extend outward.
• Common in fibrous proteins like keratin.
• Keratins: α-helix held together by hydrogen bonds and cross-linked by disulfide bridges (covalent
bonds between cysteine residues).
• Stretching hair breaks hydrogen bonds but not disulfide bridges.
• β-pleated sheet:
• Polypeptide chains line up in parallel, linked by hydrogen bonds.
• Creates a zigzag shape.
• Chains connected by hydrogen bonds between C=O and N–H groups.
• Can form between different polypeptide chains or within loops of the same chain.
• Found in fibrous proteins like silk, which is composed of β-pleated sheets.
 • Tertiary Structure:
• 3D folding of the secondary structure into a complex shape.
• Found in globular proteins (e.g., enzymes, membrane proteins, hemoglobin).
• Formed by interactions between R groups:
• Ionic attractions/repulsions.
• Polar R group reactions.
• Van der Waals’ forces between non-polar R groups.
• Hydrogen bonds with water molecules.
• Disulfide bridges lock portions of polypeptides in fixed positions.
• Sensitive to changes in temperature and pH.
• Denaturation occurs when temperature or pH changes disrupt these interactions, causing loss of
structure and function (e.g., coagulation of egg whites when cooked).

• Quaternary Structure:
• Proteins composed of two or more polypeptide chains.
• Chains are held together by:
• Hydrogen bonds.
• Hydrophobic and hydrophilic interactions.
• Positive and negative charges.
• Disulfide bridges.
• Example: Hemoglobin, which consists of multiple polypeptide subunits.
• Denaturation:
• Breakdown of tertiary structure due to changes in temperature or pH.
• Results in the unfolding of the polypeptide chain.
• Loss of biological activity.
• Examples of denaturation:
• Cooking meat or fish.
• Coagulation of egg whites.
• Curdling of milk in sunlight.
 Hemoglobin

• Hemoglobin Quaternary Structure:

• Haemoglobin is a protein with a quaternary structure found in red blood cells.
• Consists of four folded polypeptide chains (subunits).
• Held together by hydrophobic interactions, van der Waals’ forces, hydrogen bonds, and ionic bonds.
• Subunits:
• Haemoglobin has two α (alpha) subunits and two β (beta) subunits.
• Each subunit has a haem prosthetic group (iron-containing).
• Haem is located in a hydrophobic crevice, excluding water to protect Fe²⁺ from oxidation.
• Prosthetic Group (Haem):
• Non-protein component necessary for biological function.
• Haem is non-covalently bonded to haemoglobin in a hydrophobic pocket.
• Iron in haem is in the Fe²⁺ state, which binds oxygen reversibly.
• Fe²⁺ must remain unoxidized to Fe³⁺, which cannot bind oxygen.
• Binding of Oxygen:
• Each haemoglobin molecule binds four oxygen molecules.
• Binding one oxygen molecule causes a shift in the quaternary structure, enhancing oxygen binding
(cooperativity).
• As one oxygen binds, the protein’s structure changes to facilitate the binding of additional oxygen
molecules.
• The release of oxygen also causes structural changes in haemoglobin.
• Oxygenated vs. Deoxygenated Blood:
• Oxygenated blood: bright red.
• Deoxygenated blood: dark red.
• Haemoglobin A (Adult Form):
• The most common haemoglobin variant in adults.
• Consists of two identical α chains and two identical β chains.
• Each α polypeptide has 141 amino acids, and each β polypeptide has 146 amino acids.
• Haemoglobin Variants:
• Over 100 variants of haemoglobin A exist in human populations.
• Most variants are due to single amino acid changes in the β polypeptide chain, caused by mutations in
the haemoglobin gene.
 Collagen

• Function and Structure:

• Collagen is the most abundant protein in the extracellular matrix of connective tissues.
• Provides high tensile strength, giving resistance to stretch in skin, tendons, and ligaments.
e • Collagen fibres in reticular connective tissue create a netlike framework that gives shape and
structural strength to organs.
• Loose connective tissue has a low density of collagen fibres and fills spaces between organs.
• Collagen Composition:
• Made up of three polypeptide strands (microfibrils).
• Each polypeptide strand is a left-handed helix (primary structure).
• The three strands form a right-handed coil (secondary structure), stabilized by hydrogen bonds.
• The triple helix structure gives collagen high tensile strength; strands interlock and resist unwinding
under tension.
• Amino Acid Composition of Collagen:
• High proportion of glycine, proline, and hydroxyproline.
• Repeating units:
• Glycine-Proline-X (random amino acid) or
• Glycine-X-Hydroxyproline.
• Glycine appears at every third position in the primary structure.
• Glycine’s hydrogen atoms form hydrogen bonds at the interior of the helix, while the R groups of
proline and hydroxyproline are on the outside.
• Role in Wound Healing:
• Collagen fibres are exposed when blood vessels are damaged.
• Blood platelets encounter collagen, causing them to activate, swell, and become sticky.
• Activated platelets release chemicals that initiate the blood clotting process.
• Sticky platelets plug the wound and help form a blood clot to seal the wound.
• Uses of Collagen:
• Collagen is used in cosmetic surgery.
• Applied in the production of artificial skin for burn victims.

Collagen is insoluble in water, and its repeated sequences is referred to as a fibrous protein.
: Globular proteins are: Hemoglobin, Antibodies and Enzymes they are soluble in water and take part
in chemical reactions
 Part I

Part 2

Part 3

Purt y

n
e
The following are some roles of globular and fibrous proteins:
↓ - Enzymes (globular) – Lowers activation energy to catalyze certain chemical
reactions.
2 - Keratin (fibrous) – Forms protective layers and filaments, such as in hair and
nails.
3
- Insulin (globular) – Converts glucose to glycogen for storage in the cell.
Y - Elastin (fibrous) – Allows elasticity to organs such as the lungs and bladder.
 TESTING FOR REDUCING AND NON-REDUCING SUGARS

Testing for reducing sugars

Examples of reducing sugars include: GLUCOSE, MALTOSE and FRUCTOSE

Example of a non-reducing sugar is: SUCROSE.

The solution needed to test for both of these is called : BENEDICT’S

SOLUTION, a blue liquid that contains copper (II) sulphate.

Materials:

• Benedict’s solution (contains blue copper sulfate, Cu²⁺).

• Test sugar solution (1% concentration: 1 g sugar in 100 ml distilled water).
• Bunsen burner for heating.
• Test tube.

Steps for Benedict’s Test:

1. Prepare the Sugar Solution:

• Dissolve 1 g of sugar in 100 ml of distilled water to make a 1% solution.
2. Add Sugar Solution:
• Place 2 ml of the sugar sample solution into a test tube.
3. Add Benedict’s Solution:
• Add 2 ml of Benedict’s solution to the test tube containing the sugar solution.
4. Mix the Solutions:
• Gently shake the test tube to mix the sugar sample and Benedict’s solution.
5. Heat the Solution:
• Heat the test tube over a Bunsen burner, gently warming the mixture.
6. Observe Color Changes:
• If a reducing sugar is present, the solution will undergo the following color
changes as the Cu²⁺ ions are reduced to Cu⁺:
• Blue → Green → Yellow → Reddish-brown precipitate.
• The formation of a reddish-brown precipitate confirms the presence of a
reducing sugar.

Testing for non-reducing sugars

Purpose:

• To test for non-reducing sugars (e.g., sucrose) by converting them into reducing sugars.

Materials:

• Dilute hydrochloric acid (HCl).

• Sodium hydrogen carbonate (NaHCO₃).
• Benedict’s solution.
• pH paper.
• Test tube and Bunsen burner.
 Steps for Testing Non-Reducing Sugar:
sucrose

1. Hydrolyze the Sugar:

• Add the non-reducing sugar solution to a test tube.
• Add dilute hydrochloric acid.
• Boil the mixture for a few minutes to break the non-reducing sugar into monosaccharides (e.g.,
glucose, fructose).
2. Neutralize the Solution:
• After boiling, add sodium hydrogen carbonate (NaHCO₃) to neutralise the acid.
• Bubbles will form as gas is released.
• Use pH paper to check the solution is neutral (pH 7).
3. Perform Benedict’s Test:
• Add Benedict’s solution to the neutralised solution.
• Heat the test tube over a Bunsen burner.
4. Check Results:
• A reddish-brown precipitate shows that reducing sugars are present, indicating the original solution
had non-reducing sugar.

Key Point:

• The test converts non-reducing sugars into reducing sugars, which can then be detected by
Benedict’s test.

FOR NON-REDUCING SUGARS: Recall that sucrose has a GLYCOSIDIC bond. To break this
bond,
heat the solution with dilute HCl and then neutralize with SODIUM HYDROXIDE. This will yield
GLUCOSE and FRUCTOSE from the sucrose.

Testing for Starch

Testing for starch

Purpose:

• To detect the presence of starch in a solution or solid food.

Materials:

• Iodine/potassium iodide solution (I₂/KI).

• 1% starch suspension.
• Test tube.
• White tile (for solid food testing).
• Distilled water (for moistening dry solid foods).
 Steps for Testing Starch in a Solution:

1. Prepare the Sample:

• Place 2 ml of 1% starch suspension into a test tube.
2. Add Iodine Solution:
• Slowly add a few drops of I₂/KI solution to the test tube.
3. Mix the Solution:
• Gently shake the test tube to mix the contents.
4. Observe the Colour Change:
• If starch is present, the solution will immediately turn blue–black due to the formation of a
polyiodide complex.
Key Points:

• Starch is detected by the formation of a blue–black polyiodide complex.

• The test works on both liquid suspensions and solid foods.

The emulsion test Testing for lipids

Purpose:

• To detect the presence of lipids (fats) in a sample.

Materials:

• Absolute ethanol (100% ethanol).

• Cold water.
• Test tube.
• Brown paper (optional for second test).

Steps for the Emulsion Test:

1. Prepare the Sample:

• Place 2 ml of the lipid sample (or fat) into a test tube.
2. Add Ethanol:
• Add 2 ml of absolute ethanol to the test tube.
3. Dissolve the Lipid:
• Shake the test tube vigorously to dissolve the lipid in the ethanol.
4. Pour the Mixture:
• Gently pour off the alcohol/lipid solution into another test tube.
5. Add Cold Water:
• Add an equal volume (4 ml) of cold water to the solution.
6. Observe the Result:
• A cloudy white suspension indicates the presence of lipids (caused by tiny lipid droplets in the water).

Alternative Lipid Test (Brown Paper Test):

1. Rub the Sample:

• Rub the lipid sample on a clean piece of brown paper.
2. Observe the Stain:
• Hold the brown paper up to the light.
• A greasy, translucent stain indicates the presence of lipid.

Key Points:

• Lipids dissolve in ethanol but form a cloudy suspension when mixed with water.
• The brown paper test can also confirm lipids with a greasy, translucent mark.
Testing for proteins Biuret test for proteins

Purpose:

• To detect the presence of proteins by identifying peptide bonds.

Materials:

• 5% potassium hydroxide (KOH) solution.

• 1% copper sulfate (CuSO₄) solution.
• Test tube.
• Protein sample (liquid or solid).

Steps for the Biuret Test (Liquid Sample):

1. Prepare the Sample:

• Place 2 ml of the protein solution into a test tube.
2. Add Potassium Hydroxide:
• Add 2 ml of 5% potassium hydroxide to the test tube.
• Gently mix the solution.
3. Add Copper Sulfate:
• Carefully add 2 drops of 1% copper sulfate solution to the mixture.
4. Observe the Colour Change:
• A purple or violet colour indicates the presence of proteins (positive result).

Key Point:

• A purple or violet colour indicates the presence of peptide bonds, confirming the presence of
proteins.

More things to know for biochem

Carotenoids:

• Type of lipid made from isoprene units (C₅H₈).

• Light-absorbing pigments found in plants and animals.
• β-carotene:
• Traps light energy in plant leaves during photosynthesis.
• Can be broken down into Vitamin A in humans.
• Vitamin A is used to make rhodopsin, a pigment needed for vision.
• Responsible for red, orange, and yellow colours in foods like mango, carrots, pumpkins, egg yolks, and
butter.
• Present in autumn leaf colour changes and leaves of the seaside almond during the dry season.

Steroids:

• Organic compounds with multiple carbon rings in their structure.

• Cholesterol:
• Important component of cell membranes.
• Synthesised in the liver.
• Starting material for testosterone and other steroid hormones.
• Used in the production of bile salts.
• Bile salts help to emulsify dietary fats for digestion.
• Cholesterol is stored in the gall bladder and released into the duodenum when needed.
• Found in animal products like butter and milk.
• Excess cholesterol can lead to deposits in arteries, potentially causing health problems.
-
Tertiary protein

Tertiary protein

Tertiary protein
CELL STRUCTURE AND FUNCTION TOPK 2
 Functions of Membrane Systems and Organelles
Nucleus

• General Overview:
• Largest structure in plant and animal cells (~5 µm in diameter).
• Site of DNA replication and storage of genetic information.
• Controls protein production and timing.
• Key role in mitosis, ensuring hereditary information is passed to daughter cells.
• Nuclear Envelope:
• Double membrane surrounding the nucleus.
• Contains nuclear pores that allow proteins, ATP and RNA to move in and out.
• Continuous with the endoplasmic reticulum (ER), which synthesizes molecules for the cell.
• Nucleolus:
• Located inside the nucleus.
• Composed of DNA, RNA, rRNA, proteins, and ribosomal subunits.
• Site of ribosomal RNA/protein synthesis, ribosome assembly.
• Nucleoplasm:
• Viscous fluid inside the nucleus, divided into structural components and liquid cytosol.
• Contains:
• Nuclear matrix: Protein fibers and dissolved substances.
• Chromatin: DNA and histone proteins, forming chromosomes during nuclear division.
• Chromatin and Chromosomes:
• Chromatin condenses into chromosomes during mitosis.
• Haploid number of chromosomes in gametes; diploid number in somatic cells.
• Mitosis and Nuclear Envelope:
• Nuclear envelope fragments during mitosis and reforms after DNA is distributed to daughter cells.

Two types of cells that don’t have

nuclei are RED BLOOD CELLS
and PHLOEM SIEVE TUBES
Mitochondria

aerobic respiration
• General Overview:
• Sites of cellular respiration where energy is released from organic molecules like glucose.
• Size: 2–8 µm in length and 2 µm in diameter.
• Found in both plant and animal cells.
• Similar in size to bacteria and visible under a light microscope.
• Membranes:
• Outer membrane: Smooth, protective, and allows easy movement of substances. > double membrane
• Inner membrane:
• Contains numerous folds called cristae which increase surface area.
• Site of oxidative phosphorylation (ATP production via electron transport chain).
• Acts as a barrier between the cytosol and mitochondrial enzymes.
• Cristae:
• Folded structures of the inner membrane.
• Increase surface area for metabolic reactions and protein synthesis.
• Involved in electron transport and ATP synthesis.
• Matrix:
• Liquid-filled space inside the inner membrane. enzyme
Some chemical reactions
• Contains proteins, circular DNA, RNA, 70S ribosomes, and solutes. occurs in the matrix

• Site of the Krebs cycle:

• Produces carbon dioxide, ATP, NADH, and FADH₂.
• DNA and Semiautonomy:
• Mitochondria have their own circular DNA (located in the nucleoid).
• Capable of synthesizing some of their required proteins independently (semiautonomous).
• Energy Demand and Distribution:
• Number of mitochondria in a cell is related to its energy requirements.
• Mitochondria move within cells and gather where energy is needed.
• Abundant in energy-demanding cells such as:
• Cells lining the human stomach and pancreas (secreting digestive enzymes).
• Root tip cells and root hair zones in plants (absorbing water and ions).
• Human skeletal muscle cells (energy for movement).
• Human liver cells (processing nutrients and toxins).
Chloroplasts

• General Overview:
• Sites of photosynthesis in plant cells.
Has double membrane
• Contain chlorophyll and carotenoid pigments. a

• Photosynthesis converts light energy into chemical energy stored in bonds of molecules. X
• Provide energy for the plant and organisms that consume plants.
• Chlorophyll absorbs light energy and gives plants their green color.
• Chloroplast size: 4–6 µm in diameter.
• Can change position within the cell based on light intensity.
• Chloroplast Structure:
• Thylakoid Membranes:
• Internal membrane system.
• Thylakoids appear as disc-like structures stacked into grana (singular: granum).
• Site of light-dependent reactions of photosynthesis.
• Chlorophyll and carotenoids are embedded in the thylakoid membranes.
• Stroma:
• Fluid matrix surrounding the thylakoids.
• Contains 70S ribosomes and circular DNA.
• Site of light-independent reactions (Calvin cycle). Very important
• Starch granules may form temporarily during active photosynthesis.
• Chloroplast DNA and Protein Synthesis:
• Chloroplast DNA replicates independently from the cell’s nuclear DNA.
• DNA directs the synthesis of some chloroplast proteins.
• Ribosomes in the stroma synthesize proteins necessary for chloroplast function.
• Functions of Key Components:
• Thylakoid Membranes: Conduct light-dependent reactions, converting light into chemical energy (ATP and NADPH).
• Stroma: Conducts light-independent reactions (Calvin cycle), synthesizing glucose from carbon dioxide using ATP and
NADPH.

Also contains : lipids

and strack grains
Plant Cell Wall and Plasmodesmata

Plant Cell Wall:

• Overview:
• Unique to plant cells (absent in animal cells).
• Semi-rigid structure that limits protoplast size (cytoplasm and nucleus) as the cell expands due to water uptake.
• Determines cell size, shape, tissue texture, and organ structure.
• Contains enzymes involved in absorption, transport, and secretion of substances.
• Plays a role in plant defense by recognizing pathogen signals and triggering DNA activation and protein synthesis.
• Key Components:
• Cellulose: Primary component; forms the structural framework of the cell wall.
• Hemicelluloses: Polysaccharides that are hydrogen-bonded to cellulose microfibrils, providing stability.
• Pectins: Hydrophilic polysaccharides that bind water, making the wall pliable and able to expand during growth.
• Glycoproteins: Serve as structural proteins and enzymes, providing additional strength and function.
• Middle Lamella: Thin, sticky layer of pectins that cements adjacent plant cells together.
• Functions:
• Regulates cell size and shape.
• Helps with absorption, transport, and secretion of substances.
• Provides structural integrity and protection against pathogens.
• Allows the cell wall to expand as the plant grows.

Plasmodesmata:

• Overview:
• Channels that connect adjacent plant cells through the cell wall.
• Lined with the plasma membrane, making the plasma membrane continuous between connected cells.
• Structure:
• Contains cytoplasm, allowing the cytoplasm of connected cells to form a continuous network.
• Not considered organelles, but important structures for cell communication.
• Functions:
• Enable direct communication between plant cells.
• Facilitate the free passage of solutes and other small molecules between connected cells.
• Allow coordination of cellular activities across plant tissues.
Endoplasmic Reticulum (ER)

General Overview:

• Complex membrane system found in both plant and animal cells.

• Contains a narrow internal space called the lumen.
• Occupies up to 15% of a typical cell’s volume.
• Highly folded, increasing surface area significantly beyond that of the plasma membrane.
• Varies in appearance depending on cell type, metabolic activity, and developmental stage.
• Extensive in cells synthesizing proteins for export, such as glandular cells and plasma cells.

Types of Endoplasmic Reticulum:

1. Rough Endoplasmic Reticulum (RER):

• Structure: Flattened sacs called cisternae with ribosomes attached to the outer surface.
• Function:
• Protein synthesis: Ribosomes on RER synthesize proteins which enter the ER lumen.
• Protein modification: Proteins are chemically altered inside the lumen through:
• Formation of disulfide bridges.
• Folding into tertiary structures.
• Addition of carbohydrate groups for functional modification.
• Tagging proteins for specific intracellular destinations.
• Segregation: Newly synthesized proteins are separated from the cytoplasm and transported to their required locations.
• Abundance: Present in cells that store or secrete large amounts of proteins, such as digestive enzyme-secreting cells.

2. Smooth Endoplasmic Reticulum (SER):

• Structure: Lacks ribosomes on its surface.

• Function:
• Lipid synthesis: SER synthesizes lipids, including steroids.
• Detoxification: Modifies small molecules like drugs and pesticides.
• Glycogen hydrolysis: Breaks down glycogen into glucose.
• Abundance: Found in cells that secrete lipids and are involved in detoxification processes.

Connections and Continuity:

• ER is continuous with the outer membrane of the nuclear envelope.

• During mitosis (prophase), the nuclear envelope fragments and merges with the ER, becoming indistinguishable.
• After mitosis, vesicles from the ER help reform the nuclear envelope for daughter nuclei.

Key Functions of the ER:

• Protein synthesis and modification (RER).

• Lipid synthesis and detoxification (SER).
• Glycogen metabolism and steroid production (SER).
• Plays a role in the reformation of the nuclear envelope after cell division.
 • Lysosomes:
• Small organelles found in animal cells.
• Size: approximately 0.3–1 µm in diameter.
• Structure:
• Dense interior.
• Single membrane.
• Produced by the Golgi complex.
• Acidic pH (optimal for enzymatic activity).
• Functions:
• Contain hydrolytic enzymes that break down macromolecules (proteins, polysaccharides, nucleic acids, lipids) into monomers.
• Site for the breakdown of food and foreign material taken up by the cell.
• Fusion with vesicles:
• Fuses with vesicles containing materials to be digested.
• Converts contents into monomers that are released into the cytoplasm for reuse.
• Autophagy:
• Process in which the lysosome digests the cell’s own material.
• Proteins and other molecules are engulfed, hydrolyzed, and recycled back into the cytoplasm as usable building blocks (e.g.
amino acids).
• Role in Immunity:
• White blood cells engulf bacteria into vesicles, which then fuse with lysosomes to digest and destroy bacteria.
• Apoptosis (programmed cell death):
• Lysosomes contribute to apoptosis by digesting specific parts of the body (e.g. during development, lysosomes help remove
webbing between human embryo fingers).
• Centrosome:
• Paired organelle in animal cells (contains two centrioles at right angles to each other).
• Absent in plant cells.
• Also known as the microtubule organizing center (MTOC).
• Located near the nucleus.
• Centrioles:
· centrioles
• Structure:
• Small, hollow cylinders. produces
• Size: approximately 0.3–0.5 µm long and 0.2 µm in diameter.
• Composed of nine sets of three microtubules fused together.
• Microtubules are hollow, unbranched cylinders, ~25 nm in diameter. 2 microtubules
• Made of the protein tubulin.
which forms
• Function:
• Help to organize microtubules during nuclear division (important in cell division).
• Provide a framework on which motor proteins (e.g. myosin) move structures within the cell.
• Microtubules:
3
Spindle
which
• Form a rigid internal cytoskeleton in cells. helps pull chromo
Som es

• Important for maintaining the shape of animal cells (which lack a cell wall). to the
polar ends
of
coll

• Cytoskeleton: during sell division

• Provides structural support to cells.

• Serves as a scaffold for motor proteins to move various cellular components.
• Example:
• Myosin is a motor protein that moves along microtubules, especially in muscle cells.
• Golgi Complex (also known as Golgi apparatus or Golgi body):
• Found in both plant and animal cells.
• Size: approximately 1 µm long.
• Composed of flattened, membranous sacs called cisternae and small membrane-enclosed vesicles.
• Cisternae resemble a stack of saucers.
• Structure:
• Cisternae:
• Cis region: Bottom cisternae, closest to the nuclear envelope or RER.
• Medial region: Middle cisternae.
• Trans region: Top cisternae, closest to the plasma membrane.
• Different regions contain distinct enzymes and perform specific functions.
• Function:
• Receives proteins from the endoplasmic reticulum (ER).
• Chemically modifies, concentrates, and packages proteins for intracellular or extracellular destinations.
• In plant cells, the Golgi complex synthesizes and secretes cell wall polysaccharides (except cellulose).
• Vesicle Transport:
• The Golgi is not directly connected to the ER.
• ER membranes form vesicles containing proteins that travel to the Golgi complex.
• Vesicles fuse with the cis region of the Golgi, releasing proteins into the Golgi lumen.
• At the trans region, vesicles pinch off and transport proteins to their destinations.
• Vesicles may fuse with organelles or the plasma membrane to release their contents (via exocytosis).
• Vesicles:
• Small membrane-bound spheres that transport proteins.
• Shuttle proteins into and out of the Golgi complex.
• Responsible for delivering proteins to the plasma membrane or other organelles.

2 3 4
I
• Ribosome Structure:
• Small particles, approximately 17–23 nm in diameter.
• Composed of equal amounts of protein and RNA.
• Consist of two subunits:
• Small subunit.
• Large subunit.
• Subunits are produced in the nucleolus and exported to the cytoplasm for assembly.
• Location:
• Found in both plant and animal cells.
• Present in three main locations:
• Free in the cytosol.
• Attached to the endoplasmic reticulum (forming rough ER).
• On the outer surface of the nuclear envelope.
• Function:
• Site of protein synthesis: Ribosomes link amino acids together by peptide bonds to form proteins.
• Ribosomes can form clusters called polysomes (actively synthesizing proteins).
• Types:
• Eukaryotic cytoplasmic ribosomes: 80S.
• Mitochondrial and prokaryotic ribosomes: 70S.
 Prokaryotic Cells

• General Structure:
• Size: ranges from 5-10 µm
• Visible under light microscopy but with undefined sub-cellular structure.
• Lack membrane-enclosed internal compartments.
• Key Features:
• Plasma membrane: Encloses the cell.
• Nucleoid: Region in the cytoplasm containing DNA (hereditary material).
• Cytoplasm:
• Contains cytosol (water, ions, proteins, and metabolic products).
• Ribosomes (sites of protein synthesis).
• Cell Wall:
• Located outside the plasma membrane.
• Composed of peptidoglycan (a polymer of amino sugars cross-linked by covalent bonds).
• Supports the cell and determines its shape.
• Outer membrane (in some bacteria): Contains polysaccharides that may cause disease or immune responses.
• Capsule: A slime layer made of polysaccharides found on the outer surface of some bacteria.
• Mesosomes:
• Membranous structures formed by plasma membrane infolds.
• Function in protein and DNA synthesis and other metabolic reactions.
• Flagella:
• Used for movement.
• Composed of flagellin protein.
• Rotate like a propeller to drive the bacterial cell forward.

Electron Micrograph of
bacterium
 *

Endosymbiont Theory

• Concept:
• Suggests that mitochondria and chloroplasts are descendants of bacteria (prokaryotes).
• These bacteria were engulfed by an ancient host cell and became endosymbionts.
• Endosymbionts:
• Organisms that live within another dissimilar organism.
• The bacterial ancestors of mitochondria and chloroplasts had the ability to trap or convert energy, which was useful to the
host cell.
• Heterotrophic Cells:
• Heterotrophs cannot produce their own carbon-containing compounds, relying on other organisms for nutrients.
• Cells with endosymbionts gained advantages like respiration and photosynthesis capabilities.
• These cells were the ancestors of eukaryotic cells.
• Autotrophic Eukaryotes:
• Autotrophs contain chloroplasts and can make their own food by converting light energy into chemical energy via
photosynthesis.
• Dependence on Host:
• Mitochondria and chloroplasts cannot live independently of their host cells.
• Some of their required proteins are encoded in the host cell genome.
• Evidence Supporting Endosymbiont Theory:
• Chloroplasts and mitochondria are similar in size to prokaryotic cells.
• Mitochondria and chloroplasts have their own DNA but rely on the host for some metabolic needs.
 ①

M
 Tissues and Organs

• Tissues:
• A group of similar cells organized into a structural or functional unit.
• Simple tissues: Composed of one type of cell.
• Complex tissues: Composed of two or more types of cells.
• Organs:
• Structures made of different tissues performing a specific function.
• Organs are part of an organ system for efficiency and coordination of activities.
• Examples of Organ Systems:
• Respiratory system: Includes heart and lungs.
• Digestive system: Includes stomach, pancreas, gall bladder, liver, intestines.
• Root system (plants): Roots are organs.
• Shoot system (plants): Leaves are organs.

Animal Tissues and Organs

• Four principal types of tissue in animals:

1. Epithelial tissue.
2. Connective tissue.
3. Muscle tissue.
4. Nervous tissue.
• Major organs in mammals: Brain, heart, lungs, kidneys, liver, reproductive organs, skin.

Epithelial Tissue

• Structure:
• Sheets of densely packed cells covering the body and lining organs (gut, lungs, bladder, blood vessels).
• Functions:
• Secretory (e.g., mucus in lungs, digestive enzymes in stomach, sweat from skin).
• Protective: Forms boundaries between the body and the external environment.
• Specialized cells like taste receptors in the tongue.
• Regeneration:
• Epithelial cells slough off regularly (e.g., skin and gut).
• Pap smear: Diagnostic test based on shed epithelial cells from the uterus.
• Dandruff: Shed epithelial cells from the scalp.
Connective Tissue

• Collagen: Protein fiber secreted by connective tissue cells.

• Types of Connective Tissue:
• Bone: Provides rigid structural support.
• Cartilage: Strong yet flexible support material.
• Adipose tissue: Stores fat.
• Blood: Connects all parts of the body via the cardiovascular system, composed of red and white blood cells, platelets, and
plasma.

Muscle Tissue

• Function: Cells contract to cause movement.

• Types:
• Skeletal muscle: Controls body movement, connects bones.
• Smooth muscle: Found in internal organs.
• Cardiac muscle: Found in the heart.

Nervous Tissue

• Function: Processes information.

• Cells:
• Neurons: Generate electrochemical signals in response to stimuli (light, sound, pressure, etc.).
• Glial cells: Support neurones.
 • Principle Tissues of Vascular Plants:
• Grouped by their continuity throughout the plant body.
• Vascular plants: Have xylem and phloem.
• Three main tissue systems:
1. Dermal tissue system.
2. Vascular tissue system.
3. Ground tissue system.
• Major organs: Leaves, roots, flowers, stems.
• Vascular Flowering Plants:
• Divided into two groups:
1. Dicotyledons (dicots).
2. Monocotyledons (monocots).

Tissue Systems

1. Dermal Tissue System:

• Epidermis: Protective outer covering.
• Provides mechanical protection and reduces water loss from the plant surface.
2. Vascular Tissue System:
• Consists of xylem and phloem.
• Xylem: Principal water-conducting tissue.
• Phloem: Principal food-conducting tissue.
3. Ground Tissue System:
• Includes parenchyma, collenchyma, and sclerenchyma.
• Parenchyma cells: Involved in photosynthesis, storage, and secretion.
• Collenchyma cells: Provide support for young, growing organs.
• Sclerenchyma cells: Strengthen and support non-elongating plant parts.

Leaf Structure:

• Leaves are the major food-producing organs.

• Contain various tissues:
• Epidermis.
• Mesophyll.
• Parenchyma.
• Xylem and phloem.
Transverse Cross Section of a DICOTYLEDONOUS ROOT

most times it has

a cross
shape
·

⑳
Transverse section of a MONOCOTYLEDONOUS ROOT
 Membrane Structure and Function TOPIC 3

Fluid Mosaic Model:

• Membrane composed of a phospholipid bilayer with embedded proteins.

• Components are in constant motion, making the membrane fluid.

Phospholipid Bilayer: H20

• Phospholipids arrange in two layers: head

•
•
Hydrophilic heads face outward (toward water).
Hydrophobic tails face inward (away from water).
34 tails

• Provides structural integrity and impermeability to the membrane.

• In plant cells: Contains phospholipids and stigmasterol.
• In animal cells: Contains phospholipids and cholesterol.

Functions of the Plasma Membrane:

• Regulates the exchange between the external environment and the cell interior.
• Ensures optimal conditions for metabolic processes.
• Protects cell integrity and function.
• Facilitates cell coordination with others in the organism.

Proteins in the Membrane:

1. Transmembrane Proteins:
• Span the membrane, embedded in the bilayer.
• Hydrophobic part embedded in the membrane; hydrophilic parts protrude on either side.
• Play a role in transport, signaling, and cell recognition.
• Examples: Glycoproteins (with carbohydrate chains) help in hormone recognition, pathogen defense, and cell signaling.
2. Integral Proteins (Intrinsic Proteins): channel protein and carrier protein
• Tightly bound to the membrane.
• Include transmembrane proteins.
• Responsible for membrane function, such as transport and communication.
3. Peripheral Proteins (Extrinsic Proteins):
• Do not extend into the hydrophobic region.
• Attach to portions of transmembrane proteins outside the bilayer.
• Often involved in signaling or structural support.

Protein Anchoring:

• Some proteins are anchored to the cytoskeleton, leading to specialization of cell surface regions.
• Example: Synapses between motor neurons and muscle cells facilitate chemical communication due to specialized regions.

Protein Structures:

1. Rod-like structure:
• A coiled alpha-helix embedded in the membrane with hydrophilic ends extending outward.
2. Globular Complex:
• Protein spans the bilayer as a series of alpha-helices.

Membrane Dynamics:

• The fluidity of the membrane allows proteins to move, interact, and maintain function.
• Membranes can self-seal, aiding in processes like vesicle fusion and phagocytosis.
 phosphate head

acid tails
Fatty

More Functions of Cholesterol in the Phospholipid Bilayer:

• Maintains membrane fluidity:

• Prevents phospholipids from packing too closely in cold temperatures (avoids rigidity).
• Restrains phospholipid movement in high temperatures (avoids excessive fluidity).
• Provides membrane stability:
• Adds structural integrity without making the membrane too rigid.
• Reduces membrane permeability:
• Decreases permeability to small, water-soluble molecules, enhancing membrane selectivity.
 Diffusion:

• Definition: This is the net movement of molecules or ions from a region of higher to lower concentration.
• Cause: It results from the random movement of individual molecules or ions.
• Concentration gradient: Diffusion involves the movement from a region of higher concentration to a region
of lower concentration, down a concentration gradient.
• Demonstration: Adding a drop of ink to water shows diffusion as the ink molecules spread from high to low
concentration until evenly dispersed.
• Movement of water: Water molecules also move from areas of higher water potential (more water) to areas
of lower water potential (less water due to solutes).
• Independence: Ink molecules and water molecules move independently of each other.
• Equilibrium: Diffusion continues until there are no concentration gradients left, and equilibrium is reached,
meaning no net movement of molecules occurs.

Diffusion and Facilitated Diffusion are both examples of: passive transport, which means that they do not
require the use of ATP.

• Simple Diffusion:
• Molecules move directly through the phospholipid bilayer.
• Does not require any assistance from proteins.
• Movement occurs from high to low concentration (down a concentration gradient).
• Example: Small non-polar molecules like oxygen or carbon dioxide pass through the membrane.
• Facilitated Diffusion:
• Requires specific proteins (channel or carrier proteins) to assist in the movement of molecules.
• Channel proteins create hydrophilic pathways for specific molecules or ions.
• Carrier proteins bind to the molecules and undergo a shape change to transport them across the membrane.
• Still follows the concentration gradient (high to low concentration).
• Example: Movement of glucose or ions across the membrane.

Multiple factors affect rate of diffusion, such as the size of the particles as well as their charge, heat may
also increase rate of diffusion.

Facilitated diffusion mostly

happens with the
integral
proteins
 Rate of diffusion
• Simple Diffusion:
• Rate of diffusion is directly proportional to the concentration of the substance.
• As the concentration increases, the rate of diffusion continues to rise without limit.
• Facilitated Diffusion:
• Initially, the rate increases as concentration increases.
• Eventually, the rate reaches a maximum (Vmax) and plateaus.
• Reason: Facilitated diffusion depends on the availability of protein channels or carriers (like “tunnels”).
• As more substance is added, the channels become saturated, leading to a bottleneck effect, limiting the
diffusion rate.
• Factors affecting facilitated diffusion include mechanical changes, attachment of signalling molecules
(ligands), or voltage changes.
• Key Difference:
• Simple diffusion: Rate increases consistently with concentration.
• Facilitated diffusion: Rate is capped at Vmax due to limited carrier proteins.
 Active Transport
• Definition:
• Transport of substances across a membrane against a concentration or electrochemical gradient.
• Requires carrier proteins and energy, typically in the form of ATP.
• Mechanism:
• Carrier proteins in the plasma membrane are powered by ATP, causing a shape change that allows
for the movement of ions or molecules.
• Carrier proteins can function as:
• Symport: Move two substances in the same direction.
• Antiport: Move two substances in opposite directions.
• Example - Sodium-Potassium Pump:
• Pumps potassium (K+) ions into the cell and sodium (Na+) ions out of the cell.
• Maintains high K+ concentration inside the cell and high Na+ concentration outside the cell.
• Uses ATP; ATPase enzyme breaks ATP into ADP to provide energy for the pump.
• Indirect Active Transport:
• Sometimes, other molecules (e.g., glucose) can be transported along with ions like Na+ using carrier
proteins.
• This occurs without the direct use of ATP, known as indirect active transport.
• Types of Active Transport:
1. Primary Active Transport:
• Directly uses ATP to pump ions (e.g., Na+, K+) against their gradients.
• Example: Proton pump (H+-ATPase) transports protons (H+) across membranes, creating proton
gradients.
2. Secondary Active Transport:
• Does not use ATP directly.
• Utilizes the proton gradient or ion gradients established by primary active transport to move other
solutes (e.g., glucose).
• Example: The movement of sodium ions (Na+) powers the transport of glucose against its
concentration gradient.
• Energy Sources:
• Primary Active Transport: Directly uses ATP for ion pumps.
• Secondary Active Transport: Uses the electrochemical gradient created by primary transport (no
direct use of ATP).
 VESICLE-MEDIATED TRANSPORT

Definition:
• Transport of large molecules (e.g., proteins, polysaccharides) via vesicles that cannot pass through
transport proteins.
• Vesicle-Mediated Transport Process:
• Vesicles bud off from the Golgi complex and move to the plasma membrane.
• Vesicles fuse with the plasma membrane to release their contents.
• Exocytosis:
• Process by which large particles or dissolved substances are transported to the cell surface.
• Vesicle fuses with the plasma membrane and expels contents.
• Example: Mucilage on root hairs or plant cell wall matrix materials delivered via exocytosis.
• Endocytosis:
• Uptake of particulate matter or substances in bulk by the cell.
• Plasma membrane forms a pocket around the substance, creating a vesicle.
• The vesicle migrates into the interior of the cell.
• Types of Endocytosis:
1. Phagocytosis:
• Engulfs large particles or entire cells.
• Forms a vesicle called a phagosome.
• Phagosome fuses with a lysosome where the contents are digested.
• Example: White blood cells use phagocytosis to defend against pathogens.
2. Pinocytosis:
• Acquires fluids from blood via tiny vesicles.
• Brings small dissolved substances or fluids into the cell.
• Example: Occurs constantly in the endothelia of capillaries in humans.
3. Receptor-Mediated Endocytosis:
• Specific macromolecules are captured by receptor proteins on the plasma membrane.
• Receptor binds to macromolecule, and a vesicle forms, transporting it into the cytoplasm.
• Example: Cholesterol uptake by mammalian cells.
• Important Organelles Involved:
• Golgi complex: Responsible for packaging vesicles.
• Lysosomes: Contain digestive enzymes to break down phagocytosed material.
S
i
·
 Osmosis
• Definition:
• Osmosis is the net movement of water molecules from an area of higher water potential (dilute solution) to an area of
lower water potential (concentrated solution) through a partially permeable membrane.
• Selective Permeability:
• A selectively permeable membrane allows certain substances to pass while blocking others.
• Water Diffusion:
• The diffusion of water is influenced by the concentration of solutes in the solution, not by the solutes themselves.
• Types of Solutions:
• Isotonic Solutions:
• Equal solute particles per unit volume.
• Equal water potentials.
• No net movement of water unless pressure is applied.
• Hypotonic Solutions:
• Less solute (less concentrated).
• Higher water potential.
• Hypertonic Solutions:
• More solute (more concentrated).
• Lower water potential.

• Osmotic Pressure: ψ Greek symbol for water potential (psi)

• Osmosis leads to a build-up of pressure as water moves into an area of lower concentration.
• Osmotic pressure is the pressure required to stop the movement of water across a selectively permeable membrane.
• Demonstration of Osmotic Pressure:
• Use of dialysis tubing to show osmotic pressure:
• Dialysis tubing allows water but not larger molecules (e.g., proteins).
• When placed in distilled water, water diffuses into the solution inside the tubing, increasing its volume and height.
• Downward pressure (gravity) balances the upward movement of water until equilibrium is reached.
• Quantifying Osmotic Pressure:
• A piston can be used to measure the osmotic potential by applying pressure to restore the original water level.
• Example in Biological Systems:
• Blood Plasma:
• Contains salts, proteins, and organic molecules.
• Red blood cells maintain their shape in isotonic plasma.
• If pure water is added, plasma becomes hypotonic, leading to water entering the cells, causing them to swell and possibly
burst.
• Importance of Osmosis:
• Maintenance of a plasma solution that is isotonic is crucial for the integrity of red blood cells.
Potential and Osmosis in Cells:

• Water Potential:
• Represented as a negative (-) number.
• Pure water at atmospheric pressure has a water potential of zero.
• More solute in a solution results in a more negative water potential.
• Solute molecules attract water molecules, restricting their movement.
• Importance of Water in the Body:
• Approximately 60% of the human body is water.
• Water is a major component of protoplasm and cytoplasm in cells.
• Moisture lines membranes (e.g., alveoli) and is a key component of blood plasma.
• Osmosis and Cell Function:
• Regulation of water-salt balance is crucial to prevent cell damage.
• Cells can undergo:
• Crenation: Cells shrink due to loss of water.
• Lysis: Cells burst due to excessive water intake.
• Effects on Plant Cells:
• Plant cells have a cell wall, preventing lysis.
• As water enters, the cell expands, exerting pressure potential.
• If plant cells lose water:
• The plasma membrane retracts from the cell wall.
• Gaps form, and external solutions fill these gaps (cell wall is freely permeable).
• If retraction occurs completely, it can lead to cell death.
• Key Terms:
• Crenation: Shrinking of cells due to water loss.
• Lysis: Bursting of cells due to excess water intake.
• Pressure Potential: Force exerted by water entering the plant cell, contributing to turgor pressure.
Important to know
How to Determine the Water Potential of Plant Tissue: Laboratory Base Question in Exam

• Use potato cylinders as plant tissue samples.

• Submerge the cylinders in various sucrose solutions with different concentrations.
• Measure and compare the initial and final lengths/masses of the potato cylinders.
• Water will flow into or out of the potato cells depending on the water potential difference between the potato
tissue and the solution.
• If there is no change in length/mass, the water potential of the solution equals the water potential of the
potato tissue.
• Perform trials with multiple sucrose solutions and record the percentage change in mass or length.
• Graph the % change in mass/length against the sucrose concentration.
• The point where there is 0% change represents the water potential of the plant tissue.
How to Determine Solute Potential of Plant Tissue: Summary Notes Laboratory Base Question in Exam

• Solute potential (ψs): The amount by which a dissolved solute lowers the water potential.
• Relationship with water potential: The higher the solute potential, the lower the water potential. Represented
as a negative value.
• Example: 0.50 mol dm⁻³ of sucrose has ψs = -1450; 1.00 mol dm⁻³ of sucrose has ψs = -3500.
• Plasmolysis: Occurs when too much solute is in the cell, causing water to leave, the cell loses turgor, and
the cell membrane retracts from the cell wall.
• Incipient plasmolysis: The point just before plasmolysis, where the pressure potential becomes zero, and
water starts to flow out of the cell. This happens when the water potential inside equals the solute potential inside
(ψinside = ψs inside).
• Experimental aim: To observe plant tissue under a microscope in varying sucrose concentrations to
identify the sucrose concentration that acts as the tipping point for plasmolysis.
• Outcome: The higher the sucrose concentration, the more cells will become plasmolysed, with a sudden
tipping point observed.
 Enzymes TOPIC 4

• Globular proteins: Enzymes have a compact, spherical shape, allowing them to be soluble and flexible, essential for
interacting with substrates.
• Precise 3D structure: Their folded tertiary structure creates a specific active site for substrate binding.
• Active site formation: The globular structure enables the formation of an active site, where catalysis occurs.
• Dynamic nature: The flexible shape of globular proteins allows enzymes to undergo conformational changes during
substrate binding (induced fit).
• Solubility: Being globular ensures enzymes are soluble in water, making them available for metabolic reactions in the
aqueous environment of cells.
• Enzymes act as BIOLOGICAL CATALYSTS, which means that they speed up a chemical reaction. Without them,
many processes in the body would occur too slowly.

Enzymes (Proteuse)

Found in small intestine cells called intestinal

mucosa

Pepsine in Stomach
Trypsinina intestine

works best in pH
* epsine
acidic .

works best in alkaline plt.

*
Trypsin an
 How to enzymes makes it’s products :

• Enzymes bind to substrates to form an enzyme-substrate complex.

• Enzymes convert substrates into products during the reaction.
• Example:
• Starch (substrate) is broken down by amylase (enzyme) into maltose (product).
• Enzymes remain unchanged after the reaction and can be reused.
• Substrates are in constant motion due to kinetic energy, leading to collisions with enzymes.
• The active site of the enzyme contains R groups that interact with the substrate, facilitating binding and
catalysis.

Enzyme Substrate Enzyme -

Substrate Complex

Enzyme + Product

LOCK AND KEY HYPOTHESIS

• Lock and Key hypothesis: Proposes that the enzyme’s active site is a fixed, rigid structure that is perfectly
shaped to fit a specific substrate, similar to a key fitting into a lock.
↓ • Specificity: Each enzyme can only catalyze a reaction with a particular substrate due to the precise match
between the substrate’s shape and the active site.
2 • No conformational change: The enzyme’s active site is pre-shaped and remains unchanged when the
substrate binds, unlike the induced fit model where the enzyme adjusts to fit the substrate.
3 • Enzyme-Substrate Complex: The substrate (key) binds to the active site (lock), forming a temporary
complex that facilitates the chemical reaction, lowering activation energy.
Y • Catalysis: After the substrate is converted into products, it is released, and the enzyme remains intact and
ready to catalyze another reaction.
• Efficiency: This model explains the high specificity and efficiency of enzyme-catalyzed reactions, though it
has limitations for explaining more complex enzyme behaviors.
 Induced-fit hypothesis:

• Induced-fit hypothesis: The enzyme’s active site changes shape slightly to accommodate the substrate,
ensuring an optimal fit.
• Flexibility: Unlike the lock-and-key model, enzymes are flexible, not rigid. The active site adjusts to better
bind the substrate, similar to wrapping your hand around an object.
• Facilitating the reaction: The shape change of the enzyme’s active site brings the necessary protein side-
chains into alignment with the substrate, aiding catalysis.
• Reusability: After the reaction, the enzyme returns to its original shape, ready to bind another substrate
molecule.
• Example – Hexokinase: When hexokinase binds glucose, it folds around the substrate and excludes water
from the active site, promoting phosphate transfer from ATP to glucose.
• Reaction mechanisms:
• Orientation: Aligns the substrate’s atoms for bond formation.
• Charge: Adds a charge to the substrate, making it more reactive.
• Induced strain: Stretches chemical bonds in the substrate, making them less stable and more reactive.
 FACTORS AFFECTING ENZYME ACTIVITY
PH
• Enzyme activity is pH-dependent: The rate of enzyme-catalyzed reactions is influenced by the pH of
the surrounding medium.
• Optimal pH: Each enzyme has an ideal pH at which its activity is at its highest; deviations from this
optimal pH reduce activity.
• Effect of low pH (excess H+):
• Amino groups (–NH2) accept H+ and become –NH3⁺.
• Carboxylate ions (–COO⁻) combine with H+ and become –COOH.
• Effect of high pH (excess OH–):
• Carboxyl groups (–COOH) release H+ and become negatively charged carboxylate ions (–COO⁻).
• Altered charges: Changes in pH affect the charge of amino and carboxyl groups in proteins, which can
alter ionic interactions within the enzyme.
• Impact on enzyme structure: Changes in ionic interactions may modify the enzyme’s tertiary or
quaternary structure, potentially altering the active site’s shape and causing it to denature.
• Substrate changes: pH changes also affect the charges on the substrate, influencing enzyme-substrate
interactions.
 Temperature
• Temperature affects enzyme activity: Small increases in temperature generally raise the rate of enzyme-
catalyzed reactions.
• Increased kinetic energy: Higher temperatures increase the kinetic energy of both enzyme and substrate
molecules, leading to more frequent collisions and a greater chance of reaction.
• Activation energy: Increased temperature helps substrate molecules reach the activation energy required for
the reaction.
• Optimal temperature: Each enzyme has an ideal temperature at which its activity is highest; for human
enzymes, this is around 35–40°C.
• Rate doubling: The rate of enzymatic reactions typically doubles with every 10°C increase in temperature
between 10–40°C. This is called Qo temperature coefficient·
• Denaturation at high temperatures: Excessive heat (above the optimal temperature) can break bonds in the
enzyme’s protein structure, leading to denaturation.
• Denaturation effect: Changes the enzyme’s shape, preventing it from efficiently binding to substrates.
• Examples:
• Enzymes in compost heaps operate at temperatures up to 70–80°C.
• Organisms in extreme environments (e.g., hot springs or glaciers) have enzymes with different optimal
temperatures adapted to their surroundings.
 Enzyme Concentration
• Increased enzyme concentration: Generally leads to an increased rate of reaction if substrate is
available.
• More active sites: Higher enzyme levels create more active sites for substrate binding.
• Proportional increase: At low substrate concentrations, reaction rate increases with enzyme
concentration.
• Substrate saturation: Once substrates are saturated, further increases in enzyme concentration do not
significantly affect the rate.
• Optimal conditions: Must be maintained (temperature, pH) for enzyme concentration effects to be
observed.
• Application: Important for optimizing industrial processes and understanding metabolic pathways.

: Once
substrate is
NOTE saturated more

increase in enzyme
conc .
will NOT
affect
rate so the graph
will
plateau
 Substrate Concentration

Substrate Concentration Affecting Rate of Reaction

• Effect on enzyme action: Substrate concentration influences the rate of enzyme-catalyzed reactions.
• Rate increase: The rate of reaction increases with increasing substrate concentration.
• Leveling off: The rate of increase gradually levels off as substrate concentration continues to rise.
• Maximum rate: A maximum rate is reached when further increases in substrate concentration do not
significantly enhance the reaction rate.
• Enzyme saturation: At maximum rate, all enzyme molecules are bound to substrate, indicating the enzyme
is saturated.
• Enzyme vs. substrate concentration: Enzyme concentration is usually much lower than substrate
concentration; high substrate levels can exceed the enzyme’s capacity to convert substrate to product.
• Enzyme efficiency: The maximum rate of reaction reflects enzyme efficiency, measured by the number of
substrate molecules converted to product per unit time (turnover number).
• Example - Catalase: The enzyme catalase converts 40 million molecules of hydrogen peroxide to water
and oxygen per second, resulting in a turnover number of 40 million molecules/second.

NOTE : Once enzyme

conc is limited
the reaction rate
will plateau
 Competitive and Non-competitive Inhibition
Effects of Competitive and Non-competitive Inhibitors on Enzyme Activity

An INHIBITOR is a substance that will decreasethe rate of an enzyme reaction, or stop it altogether. It might do this by
preventing the substrate from binding to the active site.

Competitive Inhibition

• Definition: Competitive inhibitors compete with the substrate for binding to the enzyme’s active site.
• Structure similarity: Competitive inhibitors have a structure similar to the genuine substrate.
• Reversible: Competitive inhibition is reversible; the inhibitor can detach from the active site.
• Mechanism:
• When a competitive inhibitor binds, no catalysis occurs.
• It blocks the genuine substrate from entering the active site.
• Overcoming inhibition: Increasing the concentration of the genuine substrate can overcome competitive inhibition.
• Example:
• Succinate dehydrogenase: This enzyme converts succinate to fumarate and can be inhibited by oxaloacetate,
which competes with succinate for the active site.

Non-competitive Inhibition

• Definition: Non-competitive inhibitors bind to a site distinct(ALLOSTERIC) from the active site.
• Mechanism:
• Binding causes a conformational change in the enzyme, altering the structure of the active site.
• This can affect substrate binding and/or reduce the rate of product formation.
• Reversible: Non-competitive inhibition is also reversible.
• Effect on activity: The active site may still bind the substrate, but the overall rate of product formation is reduced.
• Examples: Common non-competitive inhibitors include heavy metals like lead, mercury, and copper.
• Types of inhibition: Enzymes can be affected by competitive, non-competitive, and irreversible inhibition.
• Cofactors: Some enzymes require non-protein molecules (cofactors) for catalytic activity.
Non-competitive inhibitors bind to ALLOSTERIC site and significantly changes active site shape while
inhibitor is binded.
Increase in the rate of substrate for a non-competitive inhibitor does not over come the inhabitation