BIOLOGICAL MOLECULES

• Living cells and organisms are made up of many

types of molecules that are essential to life. These
molecules are called as biological molecules
(biomolecules).
• Biomolecules form the building block of life. The
collection of different types of biomolecules present
in a cell is called as cellular pool.
• Cellular pool consists of organic compounds like
carbohydrates, proteins, amino acids, lipids and
nucleic acids and inorganic compounds like water,
mineral salts and gases.
• The compounds of cellular pool are classified into
two types depending upon their molecular weight and
solubility.
• Micromolecules are smaller units having low
molecular weight and high solubility. They form the
building blocks (monomers) of macromolecules, eg,
monosaccharides, fatty acids, amino acids, nucleotides
etc.
• Macromolecules are large sized molecules having
high molecular weight and low solubility. They are
formed by polymerization of micromolecules. Thus
they are polymers of micromolecules, eg,
polysaccharides, lipids, proteins and nucleic acids.
 CARBOHYDRATES
• Carbohydrates are the organic compounds which contain
the elements carbon, hydrogen and oxygen. They have the
general formula of Cn(H2O)n , where n is a variable. They
are also called as “hydrates of carbon” as hydrogen and
oxygen are present in the same proportions as in water, i.e.,
in the ratio of 2:1.
• Chemically, carbohydrates are defined as polyhydroxy
aldoses or ketoses as they contain several hydroxyl (-OH)
groups along with an aldehyde (-CHO) or a ketone (-CO-)
group. Carbohydrates containing aldehyde group are called
aldoses while that containing ketone group are called
ketoses.
• Carbohydrates are also called as saccharides (Gk.
Saccharin=sugar) as sugars are their basic components.
 Types of carbohydrates

Carbohydrates are divided into three main classes –

1. Monosaccharides
2. Oligosaccharides
3. Polysaccharides
Monosaccharides (Gk. Monos=single,saccharin=sugar) are the
simplest carbohydrates which cannot be hydrolysed further
into smaller units. They have a general formula of CnH2nOn.
They are soluble in water and sweet in taste. Depending upon
the number of carbon atoms, monosaccharides are of
following types –
i.Trioses (C3H6O3): They have three carbon atoms per molecule
ii.Tetroses (C4H8O4): They have four carbon atoms per
molecule
iii.Pentoses (C5H10O5): They have five carbon atoms per
molecule, e.g.,ribose, dexoyribose
iv.Hexoses (C6H12O6): They have six carbon atoms per
molecule, e.g.,glucose, fructose, galactose
v.Heptoses (C7H14O7): They have seven carbon atoms per
molecule
Structure of glucose: open chain form
Structure of glucose: ring form
Oligosaccharides: Oligosaccharides are
formed by condensation of 2-9
monosaccharides. Depending upon the
number of monosaccharides, they are
classified as disaccharides (e.g.,maltose,
sucrose, lactose), trisaccharides (e.g.,
raffinose), tetrasaccharides (e.g., stachyose),
pentasaccharides, hexasaccharides etc.
 Disaccharides
• Disaccharides are formed by the condensation of two
monosaccharide molecules.
• The bond formed between two monosaccharides as a result
of condensation is called as glycosidic bond, which is
normally formed between carbon atoms 1 and 4 of
neighbouring units (1,4 glycosidic bond) by losing a
molecule of water.
• On hydrolysis, they yield monosaccharides by the breakage
of glycosidic bond. This takes place during digestion of
disaccharides and polysaccharides whey they are broken
down to monosaccharides.
• Disaccharides are soluble in water and sweet in taste.
• Biologically important disaccharides are maltose, sucrose
and lactose.
 Maltose
• It is formed by condensation of two glucose
molecules.
• Two hydroxyl (-OH) groups line up alongside each
other.
• One OH group combines with H-atom from the other
to form a water molecule.
• This allows an oxygen bridge to form between two
molecules, holding them together and form a
glycosidic bond.
.
Alfa glucose Alfa glucose

Maltose
• Lactose: It is formed by condensation of one glucose
molecule and one galactose molecule.

• Sucrose: It is formed by condensation of one glucose

molecule and one fructose molecule.

• All the above disaccharides have an identical formula

C12H22O11
 Polysaccharides
• Polysaccharides are complex carbohydrates which are
formed by condensation of a large number of
monosaccharides.
• The monosaccharides are joined together by glycosidic
bonds with a loss of water each time a monosaccharide
molecule is added.
• They are long chained structures, which may be linear,
branched or unbranched.
• They are inloluble in water and sweetness is absent.
• Upon hydrolysis, polysaccharides yield monosaccharides.
• The most important polysaccharides are starch, cellulose
and glycogen, all of which are polymers of glucose.
• Starch: It is a polymer of α glucose molecules. It is a
mixture of two substances – amylose and amylopectin.

• Amylose: It is formed by condensation of many α glucose

molecules that are joined with each other by 1,4 glycosidic
bonds. In this way a long, unbranched chain of several
thousand glucose molecule is build up. They are linked
between carbon atoms a1 and 4 of successive glucose units.
The chains are curved and coil up into helical structures
making the final molecule more compact. Thus amylose is
an unbranched but spirally coiled chain of several thousand
glucose units.
• Amylopection: It is formed by condensation
of many α glucose molecules that are joined
with each other by 1,4 and 1,6 glycosidic
bonds. Branches are formend by 1,6
glycosidic bonds. Thus amylopectin is a
much branched chain of several thousand
glucose units.
Amylose
Amylopectin
• Glycogen: It is very similar to amylopectin
formed of several α glucose molecules joined
by 1,4 and 1,6 glyocosidic bonds. However it
shows more branching than amylopectin.
Thus glycogen molecule is long, much
branched chain of about 30000 glucose units.
 Cellulose
• It is a polymer of β glucose.
• It is formed by condensation of many β glucose
molecules that are joined with each other by 1,4
glycosidic bonds forming a very long unbranched
structure.
• Several molecules (glucose polymers) are held
together by hydrogen bonds to form cellulose
microfibrils which are arranged in larger bundles in
plant cell walls
• In β glucose, the –OH group on carbon atom 1 projects
above the ring. In order to form a glycosidic bond with
carbon atom 4, where the –OH group is below the ring, one
glucose molecule must be upside down relative to the other,
that is rotated by 180o.
• Thus successive glucose units are linked at 180o to each
other.
• The –OH groups project outwards from each chain in all
directions and forms hydrogen bonds with neighbouring
chain. This is called cross-linkage that binds the chains
rigidly together.
 Functions of carbohydrates
1.Triose sugars (glyceraldehydes and dihydroxyacetone) are
important intermediates of both respiratory and photosynthetic
pathways.
2.Tetrose sugar (erythrose) is also an intermediate of respiratory
and photosynthetic pathways. It also acts as a raw material for
the synthesis of lignin, anthocyanin and some amino acids.
3.Pentose sugars (ribose and deoxyribose) are the
constituentsof DNA and RNA. Synthesis of ATP and some
coenzymes also requires ribose sugar.
4.Hexose sugars (glucose) is the most common respiratory
substrate.
5.Monosaccharides are polymerized to form oligosaccharides
and polysaccharides.
6.Fats and amino acids are formed from glucose and
other sugars.
7.Starch and glycogen are the major food reserves of
plants and animals respectively. On hydrolysis, these
storage carbohydrates provide energy.
8.Cellulose is the structural carbohydrate of cell wall of
plants.
9.Some plants store oligosaccharides as reserve food,
e.g., sucrose in sugarcane.
10.Oligosaccharides attached to cell membranes take
part in recognition, attachment and antigen specificity.
 Lipids
• Lipids (Gk. Lipos=fat) are the organic compounds
made up of carbon, hydrogen and oxygen.
• Content of oxygen is always small as compared to
carbon and hydrogen. Thus they need large amount
of oxygen for their oxidation to release energy.
• They are insoluble in water but soluble in a number
of organic solvents like ether, benzene, chloroform,
acetone etc.
• True lipids are formed by condensation reaction
between fatty acids and alcohol.
• Fatty acids: These are organic acids having
hydrocarbon chain that end in an acidic carboxylic
group.
• They have the general formula of R.COOH, where R
is hydrocarbon chain such as - CH3, -C2H5 and so on
increasing by - CH2 for each subsequent member of
the series and COOH is an acidic carboxylic group.
• Fatty acids are of two types – unsaturated and
saturated.

• Alchols: Most lipids are made from the alcohol

glycerol.
Saturated and unsaturated fatty acids
 Saturated fatty acids Unsaturated fatty acids
They lack double bonds They contain one or more
between neighboring double bonds between
carbon atoms. neighboring carbon atoms
(C=C)
They are solid at room They are liquid at room
temperature. temperature
Example: animal lipid Examples: Plant lipids like
sunflower oil, mustard oil
etc.
 Classification of lipids
Lipids are classified into three types – simple, compound
and derived.
1.Simple lipids are made from fatty acids and alcohol without
any additional group. They are further classified into
following types:
i. Neutral fats ii. Oils iii. Waxes
2.Compound or conjugated lipids possess additional groups
besides fatty acids and alcohol, e.g., phospholipid,
glycolipid, lipoprotein etc.
3.Derived lipids include hydrolysed products of simple and
compound lipids.eg, steriods like cholesterol, diosgenin etc.
 Neutral fats: They are formed by
condensation reaction between fatty acids
and glycerol and are thus called glycerides.
Depening upon the number of fatty acids,
they are called as monoglyceride, diglyceride
or triglyceride.
• Monoglyceride (one glycerol + one fatty acid)
• Diglyceride (one glycerol + two fatty acids)
• Triglyceride (one glycerol + three fatty acids)
• Triglycerides are the most common types of lipids
formed by condensation reaction between one
molecule of glycerol with three molecules of fatty
acids by removing three molecules of water.
• The bond formed between fatty acids and alcohol is
called as ester bond.
• They are insoluble in water but soluble in certain
organic solvents.
• They are non polar and hydrophobic.
• They consist of glycerol head and three fatty acid
tails.
• Oils: These are fats rich in unsaturated fatty acids
and are thus liquid at room temperature.
• Waxes: These are formed by fatty acids and
alcohol other than glycerol. Plant waxes occur in
cutile (along with cutin) which reduces the rate
of transpiration. In animals, cutaneous glands
secrete wax which forms a protective water
insoluble coating on animal fur.
• Phospholipid is a special type of lipid containing a
phosphate group.

• It is formed of condensation reaction between one

glycerol with two fatty acids and a phosphoric acid.

• Phospholipid is the basic structure of cell membrane.

It has hydrophilic head of phosphate and hydrophobic
tail of two fatty acids. This is very essential in the
formation of membrane.
 Functions of lipids
1.A major function of lipids is to act as energy stores. They
have a higher energy value than carbohydrates. They yield
twice as much energy per gram as compared to
carbohydrates.
2.They form an insulating layer below the dermis of skin of
vertebrates for protection against low temperatures. It is
extensive in mammals living in cold climates.
3.They act as solvent for fat soluble vitamins like A,D,E and K.
4.Fats can be converted in carbohydrates. Therefore, fats
stored in oil seeds (e,g., mustard, sunflower, cotton) not
only provide energy but also act as raw materials for
growth of embryo.
5.Phospholipids and glycolipids are the components of cell
membrane.
6.Edible oils extracted from many seeds are used in
cooking.
7.Waxes form a protective layer over the animal fur. In land
plants they reduce the rate of transpiration. They
protect the floating leaves of aquatic plants against
wetting.
8.When fats are oxidized, water is released as a product.
This metabolic water can be very useful to some desert
animals, such as camel. It stores fat in its hump primarily
as a water source rather than an energy source.
9.Cholesterol, on exposure to UV-rays form vitamin D.
10.Diosgenein is used in making anti fertility pills.
 Amino acids
Amino acids are the building blocks of
proteins. Over 170 amino acids are known to
occur in cells and tissues, out of which only 20
are commonly found in proteins. Out of these
20 amino acids, 8 are essential which are not
synthesized in the body and thus must be
included in diet while 12 are non-essential
amino acids which are synthesized in the body.
However, plants are able to make all the amino
acids they require. The general formula of
amino acid is –
All amino acids have a central carbon atom known
as α carbon atom, to which is always attached an
acidic carboxylic group (-COOH), a basic amino
group (-NH2), a hydrogen atom (H) and an alkyl
group (R). Alkyl group is also called side chain
which is different in different amino acids. Thus
alkyl group gives each amino acid its uniqueness.
20 different amino acids
 Acidic, basic and neutral amino acids
• Amino acids containing more than one acidic
carboxylic group are called as acidic amino
acids.

• Amino acids containing more than one basic

amine groups are called as basic amino acids.

• Amino acids containing one acidic carboxylic

group and one basic amine groups are called
as neutral amino acids.
 Peptide bond
Peptide bond is formed when a molecule of water is
removed during a reaction between the amino group
of one amino acid and the carboxyl group of another
amino acid. Removal of water is known as
condensation and the bond formed is called as
peptide bond. The new molecule thus formed is
called a dipeptide, which possesses a free amino
group at one end and a free carboxyl group at the
other end. This enables further combination
between the dipeptide and other amino acids. If
many amino acids are joined together in this way, a
polypeptide is formed. Upon hydrolysis (i.e. addition
of water), polypeptide can be broken down to amino
acids.
 Functions of amino acids
1.Amino acids are building blocks of proteins and enzymes.
2.Amino acid tryptophan produces plant hormone indole 3-
acetic acid (IAA) and vitamin nicotinamide.
3.Hormones thyroxin and adrenaline are formed from animo
acid tyrosine. It also give rise to a skin pigment melanin.
4.Histamine, which is required for functioning of muscles, is
derived from amino acid histidine.
5.Some amino acids, e.g., methionine act as donors of
methyl group in the synthesis of various organic
compounds including alkaloids.
6.Excess amino acids are changed to glucose in liver or used
directly in metabolism.
 Proteins
Proteins are macromolecules having one or more
polypeptides (chains of amino acids). Thus proteins are the
polymers of amino acids. They always contain the elements
carbon, hydrogen, oxygen and nitrogen and in some cases
sulphur. There are 20 different amino acids which are
commonly found in naturally occurring proteins. The
variety of proteins is unlimited because the sequence of
amino acids in each protein is specific and is genetically
controlled by DNA. Proteins are the most abundant organic
molecules to be found in cells. They are an essential
component of the diet of animals and may be converted to
both fats and carbohydrate by the cells. They show a great
range of structural and metabolic activities within the cells.
 Structure of protein
• There are four separate levels of structure and
organization of proteins as follows-

i.Primary structure: It is the description of basic

structure of a protein. This includes number of
polypeptide chains in a protein as well as number and
sequence of amino acids in each polypeptide chain. The
sequence of amino acids of a protein is genetically
controlled by the sequence of bases in DNA. Eg, insulin
is a protein made up of 51 amino acids. It is made up of
two polypeptide chains held together by disulphide
bonds.
ii. secondary structure: In addition to primary
structure there is a specific secondary
structure. It is the development of new stearic
relationships of amino acids present in the
linear sequence inside the polypeptides. There
are three types of secondary structure – α
helix, β pleated and collagen helix.
Alfa helix: In this type, the polypeptide chain is
spirally coiled and its structure is maintained
by hydrogen bonds which are formed
between oxygen of CO group of one amino
acid and hydrogen of NH group of next fourth
amino acid. Thus first amino acid would be
bonded to fifth amino acid, second amino acid
to sixth amino acid and so on. Α helical
secondary structure is found in several
proteins like keratin (hair), myosin (muscle),
epidermin (skin) etc.
• Β pleated: In this type, two or more
polypeptide chains get interconnected by
hydrogen bonds. They are arranged in parallel
fashion, either running in the same direction
or in opposite directions. Thus a β pleated
structure produces a sheet instead of a fibre
or rod as in α helix. Hydrogen bond is formed
between CO and NH groups of adjacent
chains. Β pleated structure is found in a
protein fibrion that makes silk.
• Collagen helix: In this type, there occur three
strands or polypeptide chains that are spirally
coiled around each other to form a triple helix.
The three strands are held together by
hydrogen bonds. Each chain is in the form of a
loose helix. Many triple helicases can lie
parallel to form fibrils, which in turn unite to
form fibres.
• iii.Tertiary structure: It is formed by extensive
bending and folding of a polypeptide chain
forming a precise, compact globular shape.
Tertiary structure is maintained by the
interaction of the various types of bonds
namely ionic bonds, hydrogen bonds,
disulpide bonds and hydrophobic interactions.
These bonds can be easily broken by high
temperature, drastic changes in pH and salts
of heavy metals. This process of degrading the
tertiary structure is known as denaturation.
• iv.Quaternary structure: Many highly complex
proteins consists of more than one
polypeptide chains. The different chains are
held together by hydrophobic interactions,
hydrogen bonds and ionic bonds. Their precise
arrangement is known as the quartenary
structure. Haemoglobin, consisting of four
polypeptide chains, shows quartenary
structure.
 Types of proteins: Proteins are classified into various
types on the basis of their shape, function and
composition.

i.On the basis of shape: Depending upon their

shape, proteins are classified as fibrous and globular.

• Fibrous proteins: These are thread like proteins

which may occur singly or in groups. They are tough
structural proteins. They are insoluble in water. They
generally possess secondary structure, e,g., keratin of
skin and hair. Some fibrous proteins are contractile,
e.g., myosin of muscles.
Globular proteins: They consist of one to several
polypeptide chains which are twisted irregularly giving a
rounded structure. They possess tertiary or quaternary
structure. They may be enzymatic or non-enzymatic.
Smaller globular proteins are soluble in water and are not
coagulated by heat while larger ones are easily
coagulated by heat. Egg albumin, serum globulins and
glutelins (rice, wheat) are some larger globular proteins.
 ii.On the basis of function: Depending upon their
function, proteins are classified as enzymatic and non-
enzymatic.

• Enzymatic proteins: They function as enzymes, which

catalyze various metabolic reactions. They are usually
globular, e.g., amylase, lipase etc.

• Non enzymatic proteins: They may be structural or

storage proteins. Structural proteins form part of cellular
structure and may be globulr or fibrous, e.g., cell
membranes. Storage proteins occur as food reserve
mostly in seeds, eggs or milk. They are usually globular,
e.g., albumins, globulins etc.
• iii.On the basis of composition: Depending on their
composition, proteins are classified as simple, conjugated
and derived.

• Simple proteins: They are made up of amino acids only

without any non-amino group,e.g., histones, keratin etc.

• Conjugated proteins: They are made up of non-amino

prosthetic groups in addition to amino groups, e.g.,
nucleoproteins, lipoproteins, glycoproteins etc.

• Derived proteins: They are derived from proteins through

denaturation, coagulation and breakdown,e.g., fibrin
 Functions of proteins
1. Structural proteins- They take part in formation of colloidal
complex of protoplasm, cell organelles, cell membranes
etc. Many proteins form supporting structures like elastin
of ligaments, collagen of tendons, cartilage, bone and
connective tissue.
2.Carrier proteins- A number of carrier proteins occur in the
cell membranes for transporting specific materials inside
the cell, e.g., glucose, amino acids etc. Similarly,
haemoglobin of RBCs transports oxygen from lungs to
different parts of the body.
3. Enzymes- Most of the enzymes are proteins that catalyze all
the metabolic reactions in the cells.
4.Hormones- Some hormones are proteins, e.g., insulin that
regulates sugar metabolism.
5. Antibodies- They are made up of proteins which help in
defensive mechanism of cells. Antibodies are meant for
recognizing and neutralizing toxins, viruses and other
pathogens.
6. Actin and myosin are fibrous proteins which form the
contractile system of muscles.
7. Rhodopsin and iodopsin are protein pigments present in
the rods and cones of retina that take part in perception of
image.
8. Caesin of milk, glutelin of cereals, albumin of egg are
storage proteins.
9. Fibrinogen and thrombin are blood clotting proteins that
prevent loss of blood from injured vessels by causing
clotting of blood.
 Nucleic acids
• Nucleic acids (DNA and RNA) are the genetic materials of
living organisms. They were first isolated by Miescher
(1868) from the nuclei of pus cells and were named as
nucleic acids by Altmann (1889). They are complex
molecules containing carbon, hydrogen, oxygen, nitrogen
and phosphorus. They are macromolecules formed by a
large number of repeated units called nucleotides. Thus
they are polymeric compounds containing nucleotides as
monomers and are thus called as polynucleotides.

• Nucleotides: Nucleotides are the monomers of nucleic

acids. A nucleotide is a condensation product of three
components – phosphoric acid, pentose sugar and nitrogen
base
• Phosphoric acid (biologically called as phosphate)
gives nucleic acids their acidic characters.
• Pentose sugar: It is the sugar containing five carbon
atoms. It is of two types – ribose sugar and
deoxyribose sugar. Deoxyribose sugar is similar to
ribose sugar except it has one oxygen atom lesser in
its molecule. Ribose sugar occurs in RNA while
deoxyribose sugar occurs in DNA.
• Nitorgen base: It is of two types – purines and
pyrimidines. Purine(double ringed structure) is of
two types – Adenine (A) and Guanine (G) while
pyrimidine(single ringed structure) is of three types
– Cytosine(C), Thymine (T) and Uracil(U)
• A combination of a nitrogen base with a pentose sugar is
known as nucleoside. A nucleoside when combines with a
phosphate forms a nucleotide.
Nitrogen base + Pentose sugar = Nucleoside
Nucleoside + Phosphate = Nucleotide

• Nucleotides in DNA are called as deoxyribonucleotides

while those of RNA are called as ribonucleotides.

• Depending upon the types of nitrogen bases, different

types of nucleosides and nucleotides occur in DNA and
RNA as follows –
Nitrogen Nucleosides Nucleotides
base
Deoxyribonucleoside Ribonucleoside Deoxyribonucleotide Ribonucleotide

Adenine Deoxyadenosine Adenosine Deoxyadenosine Adenosine

monophosphate monophosphate

Guanine Deoxyguanosine Guanosine Deoxyguanosine Guanosine

monophosphate monophosphate

Cytosine Deoxycytidine Cytidine Deoxycytidine Cytidine

monophosphate monophosphate

Thymine Deoxythymidine Deoxythymidine

monophosphate
Uracil Uridine Uridine
monophosphate
 Deoxyribonucleic acid (DNA)
• DNA is the principal genetic material of living
organisms. In eukaryotes, it lies inside the
nucleus. Small amount of DNA is also present in
mitochondria and plastids. In prokaryotes, DNA
lies freely in the cytoplasm. Nuclear DNA is
associated with histone protein to form
chromatin fibres which condense into
chromosome during nuclear division. Extra
nuclear DNA (as found in mitochondria, plastids
and prokaryotes) is not associated with histone
protein. It is thus naked and commonly circular.
 Watson and Crick model of DNA
James Watson and Francis Crick proposed a model of DNA in 1953
and for this discovery they were awarded a Nobel prize in 1962.
According to them, DNA has the following structural features –

1.DNA consists of two polynucleotide chains each composed of

deoxyribonucleotides as monomers.
2.Each chain forms a right-handed helical and the two chains coil
around each other to form a double helix around the central axis.
3.In each chain, the successive deoxyribonucleotides are linked to one
another by phosphodiester bonds
4.The chains run parallel but in opposite directions, that is they are
antiparallel.
5.Each chain has a sugar-phosphate backbone with nitrogen bases
which project at the right angles.
6.Two chains are held together by weak hydrogen bonds
between specific pairs of purines and pyrimidines. Purine
of one chain pairs with pyrimidine of other chain.
Adenine always pairs with thymine with two hydrogen
bonds while cytosine always pairs with guanine with
three hydrogen bonds. They are called as complementary
base pairs.
7.Two chains are separated by 20Ao distance.
8.The helix takes a complete turn after 34Ao.
9.There are ten nucleotides in each turn of DNA. Thus the
adjacent nucleotides occur at a distance of 3.4Ao.
Watson and Crick model of DNA
 Functions of DNA
1.DNA is the genetic material of living organisms which
carries all the hereditary information.
2.It give rise to new DNA by the process of replication and
this is very essential for the transfer of genetic information
from cell to cell and from generation to generation.
3.It give rise to RNAs through the process of transcription.
4.It plays a major role in protein synthesis. Proteins may
have structural or enzymatic roles.
5.Any change in the sequence and number of nucleotide of
DNA causes mutations which are the foundation of
variations and evolution.
 Ribonucleic acid (RNA)
• Unlike DNA, RNA is normally a single stranded,
non-helical polynucleotide chain. RNA chain is
composed of a number of ribonucleotides as
monomers. Successive ribonucleotides are linked
together by phosphodiester bonds. RNA
polynucleotide chain consists of ribose sugar and
phosphoric acid alternating with each other with
nitrogen bases at right angles.
• RNA is formed through transcription of DNA. RNA
is not the hereditary material except in some
viruses which lack DNA, e.g., TMV, HIV,
bacteriophages.
 Types of RNA
1.Messenger RNA (mRNA): It constitutes about 3-
5% of the total RNA of the cell. It is the longest of all
RNAs. It is a single stranded molecule formed on a
single strand of DNA inside the nucleus by a process
of transcription. The process is catalyzed by an
enzyme RNA polymerase II. The function of mRNA is
to carry genetic information for protein synthesis
from DNA to ribosomes in the form of codons
(codon=a sequence of three nitrogen bases that
specify a particular amino acid in protein).
2.Ribosomal RNA (rRNA): It makes up about 80%
of the total RNA of the cell. It is synthesized by
DNA of nucleolus by the process of transcription.
The process is catalyzed by an enzyme RNA
polymerase I. rRNA is the major component of
ribosome. It is associated with protein molecules
which together form ribosomes. Ribosomes are
the sites of protein synthesis.
3.Transfer RNA (tRNA): It makes up about 15% of
the total RNA of the cell. It is the smallest of all the
RNAs having 70-90 nucleotides per molecule. It is
synthesized by DNA inside the nucleus by the
process of transcription and the process is
catalyzed by an enzyme RNA polymerase III. tRNA
transfers amino acid from cytoplasm to ribosome
for protein synthesis. Each amino acid has its own
specific tRNa.
 Strucutre of tRNA

• All tRNA molecules have the same basic structure.

Holley (1969) proposed the clover leaf model of
tRNA. According to this model, the single stranded
polynucleotide chain of tRNA is twisted and folded
over itself to form five arms and appears to be a
clover leaf shaped structure. It has the following
structural features-
1.The 5-end of tRNA always ends in the base guanine while its 3-end
always ends in the base sequence of CCA. It is the site for binding
tRNA with specific amino acid.
2.Away from 3-end, the first loop is the ribosomal binding loop which
helps in binding tRNA with ribosome and consists of seven bases.
3.The extra loop is variable in nucleotide composition and is lacking
entirely in some tRNA.
4.The lowermost loop is anticodon loop consisting of seven bases and
permits temporary complementary pairing with codon of mRNA.
Anticodon loop of tRNA recognizes the codon of mRNA and gets
attached to it at the time of protein synthesis.
5.Away from 5-end. The first loop is the amino acyl synthetase
binding loop which consists of 8-12 bases and help in binding the
specific amino acid activating enzyme to tRNa.
Structure of tRNA
Differences between DNA and RNA
 Minerals
• Minerals are the substances present in the earth’s crust. The
minerals that are useful to organisms are called essential elements
or essential minerals. An essential mineral is that which is required
for nutrition, growth, development or functioning of organisms.
Depending upon their concentration required, essential minerals are
differentiated into two categories – major and minor (in case of
animals) or macronutrients and micronutrients (in case of plants)
• Major minerals: Calcium, Phosphorus, Sodium, Chlorine,
Magnesium and Sulphur.
• Minor minerals: Iron, Copper, Cobalt, Manganese, Molybdenum,
Zinc, Fluorine, Iodine and Selenium.
• Macronutrients: Phosphorus, Potassium, Calcium, Magnesium,
Sulphur and Iron. C, H and O are also macronutrients but are not
generally derived from minerals.
• Micronutrients: Manganese, Cobalt, Zinc, Boron, Copper,
Molybdenum and Chlorine
 Functions of minerals
• Calcium (C): Calcium provides strength and rigidity to bones and
teeth. It also plays a role in blood clotting. Calcium ion (Ca++) assists in
muscle contraction. The exoskeleton of invertebrates is strengthened
by deposits of calcium salts. Shells of molluscs are made up of
calcium carbonate. Calcium pectate is a component of middle lamella
in plant cells.
• Magnesium (Mg): Magnesium strengthens the bones and teeth. It is a
component of chlorophyll molecules. It is also a co-factor of enzymes
like ATPase. It is essential for binding the components of ribosomes
during protein synthesis. Magnesium ion (Mg++) also help in muscle
contraction.
• Potassium (K): Potassium (K+) along with Sodium (Na+) ions maintains
electrical potential across the cell membranes. They also take part in
conduction of nerve impulse. Potassium ion(K+) is involved in active
transport, opening and closing of stomata, synthesis of nucleic acid
and chlorophyll etc.
• Sulphur (S): Sulphur-containing amino acids are components of some
proteins, e.g., keratin. Sulphur is also a component of organic
compounds, e.g., Co-enzyme A.
• Sodium(Na): Sodium (Na+) and Potassium (K+) ions maintain the
osmotic balance of cellular fluids. It also takes part in conduction of
nerve impulse. Sodium also acts as co-factor in photosynthesis and
respiration.
• Nitrogen(N): Nitrogen is a component of proteins, nucleic acids and
organic compounds. It is also a component of chlorophyll.
• Phosphorus (P): Phosphorous occurs in the cell membranes, in the
ribosomes and in the chromosomes, in the nucleotides, in the energy
carriers, such as ATP, in the coenzymes such as NADP and in the
nucleic acids (DNA and RNA). It is also a constituent of enamel of
bone and teeth.
• Chlorine (Cl): Chlorine forms a major component of blood plasma. It
also helps in exchange of gases in tissue during respiration (chlorine
shift).
• Copper(Cu): Copper is a co-factor of the enzyme cytochrome oxidase.
It also helps in the production of melanin.
• Iron(Fe): Iron-containing respiratory pigment haemoglobin of the red
blood corpuscles carries oxygen from the respiratory surface to the
various cells of the body. The oxygen storing pigment myoglobin of
muscle cells also contains iron. Iron is a co-factor of the enzyme
cytochrome. Iron is also a component of chlorophyll and carotenoids.
• Iodine(I): Iodine controls general metabolism as a part of thyroxine
hormone. Its deficiency in diet depresses thyroid activity and
enlarges the thyroid gland causing goitre.
• Manganese(Mg): Manganese ions help the enzymes that catalyze the
synthesis of oligosaccharides and glycoproteins. It also helps in
oxidation of fatty acis.
 Water
• Water is the most abundant inorganic compound
in majority of cells. It forms about 60-90% of the
cell contents. It is an essential compound for the
maintenance of life. Without water, life could not
exist on this earth. It is important for two reasons.
Firstly it is a vital chemical constituent of living
cells, and secondly it provides an environment for
those organisms that live in water.
 Structure
Water molecule is formed by the combination of two
hydrogen atoms and one oxygen atom. In water, one part,
or pole, of the molecule is slightly positive and the other
slightly negative. This is known as dipole. It occurs
because the oxygen atom has greater electron-attracting
power than then the hydrogen atoms. As a result the
oxygen atom tends to attract the single electrons of the
hydrogen atoms. Electrons are negatively charged, so
giving the oxygen atom a slightly negative charge relative
to the hydrogen atom. Water molecules therefore have a
weak attraction for each other, with opposite charges
coming together called as hydrogen bonds.
 Biological significance of water
`
1. Water as a solvent: Water is an excellent solvent for polar
substances. These include ionic substances like salts, which
contain charged particles (ions), and some non-ionic
substances like sugars that contain polar groups (slightly
charged) such as the slightly negative hydroxyl group (-OH).
On contact with water, the ions and the polar groups are
surrounded by water molecules which separate (dissociate)
the ions from each other and separate them. Once a
substance is in solution, its ions can move more freely thus
making it chemically reactive. Thus majority of chemical
reactions of cells take place in aqueous solution.
2. Water as a transport medium: Water is the
transport medium in circulatory, digestive and
excretory systems of animals and in vascular
tissues in plants.
3.Thermal properties

A. Specific heat capacity: As hydrogen bonding restricts

the movement of water molecules, a relatively large
amount of energy is needed to raise the temperature of
water (i.e. water has very high specific heat capacity).
This means large bodies of water such as oceans and
lakes are very slow to temperature change as
environmental temperature changes. This makes them a
suitable habitat for aquatic organisms. Due to large
proportion of water in the body, internal changes in
temperature are also maintained, making it easier to
achieve a stable body temperature.
B.Latent heat of vaporization: Large amount
of energy is required to convert water into
vapour (i.e. water has very high latent heat of
vaporization). As a result a lot of heat is lost
during evaporation of sweat making it an
effective means of cooling in the body.
C. Latent heat of fusion: Water freezes only
when it loses large amount of energy (i.e.
water has very high latent heat of fusion). This
protects the living cells from getting frozen
even when the exterior is very cold.
3.Density and freezing properties: Water is
an unusual chemical because the solid form
i.e. ice is less dense than its liquid form. Below
4oC density of water starts to decrease. Ice
therefore floats on water and insulates the
water under it. This reduces the tendency for
large bodies of water to freeze completely,
and increases the chances of life surviving in
cold conditions.
4.High surface tension and cohesion:
Cohesion is the force whereby individual
molecules stick together. At the surface of a
liquid, a force called surface tension exists
between the molecules as a result of cohesive
forces between the molecules. High surface
tension and cohesion of water molecules is
important in translocation of water through
xylem in plants where water moves in long,
unbroken column.