NEET 2025 LECTURE NOTE - BIOLOGY [FIRST YEAR]

CHAPTER 05
BIOMOLECULES

CONTENTS :

- Introduction

- Secondary metabolites

- Carbohydrates

- Proteins

- Lipids

- Nucleic acids

- Concept of metabolism

- Living state

- Enzymes

Biomolecules are the molecules present in the living system ( protoplasm ). They are essential
for the metabolic activities and for the existence of life. So called as metabolites.

All biomolecules present in protoplasm forms a cellular pool. About 40 different elements
present in it.

O > C > N > H are the most important elements of the living world.

Element % Wt in the earth crust % Wt in human body

Oxygen 46.60% 65%
Carbon 0.03% 18.50%
Nitrogen negligible 3.30%
Hydrogen 0.14% 0.50%

Biomolecules may be organic or inorganic. An ash test helps to seperate them.

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Based on the molecular weight biomolecules are two types, micro and macro.

An acid fraction test with trichloro acetic acid ( Cl3CCOOH ) helps to seperate macro and
micro biomolecules.

Lipid is a micromolecule (wt less than 800 Da) but present in the retentate

Average composition of cells

Biomolecules % Wt in protoplasm
Water 70 - 90%
Protein 10 - 15 %
Nucleic acids 5-7%
Carbohydrates 3%
Lipids 2%
Inorganic ions 1%

Metabolites

There are some metabolites that are involved in growth and development and are known as
primary metabolites.

Eg: Aminoacids, Lipids etc.

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Some biomolecules have no major role in metabolism of the producer, are known as secondary
metabolites. They are generally present in plants ( absent in animals ). Most of the secondary
metabolites are useful to human welfare.

Pigments Anthocyanin, carotinoids

Alkaloids Morphine, codein, nicotine
Drugs Vinblastin, curcumin, reserpine
Oils Lemongrass oil, Gingelly oils
Terpenoids Monoterpens, diterpenes
Toxins Ricin, abrin
Polymeric substances Rubber, gums, Cellulose
Lectins Concanavalin-A

CARBOHYDRATES

The organic biomolecules formed from C,H and O in 1:2:1 ratio. Carbohydrates are the main
energy providers of living system.

Monosaccharides (CnH2nOn)

Simple sugars which cannot hydrolyse in to other sugar molecules.

Example: 1) Glyceraldehyde and Dihydroxy acetone (Triose sugars)

2) Ribose and Ribulose (Pentose sugars)

3) Glucose and Fructose (Hexose sugars)

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Glucose
Glucose is a hexose, aldose, reducing sugar. also known as Grape sugar , Blood sugar.

Fructose
Fructose is a hexose, ketose, reducing sugar

It is the sweetest known sugar and mainly present in fruits ( fruit sugar )

Present in seminal plasma.

Disaccharides
The group of carbohydrates formed from two monosaccharides. They are linked by glycosidic
bond. It is a C - C bond formed through dehydration ( condensation )

Maltose
Maltose is a reducing sugar formed by condensation of two glucose units.

In maltose the glucose units are connected by   1 - 4 glycosidic linkage.

Lactose
It is a reducing sugar formed from one glucose unit and one galactose.

Sucrose
Sucrose is a disccahride of glucose and fructose. .Sucrose is the main transporting form of
carbohydrate in plants because of its non reducing nature.

Polysaccharides
Polysaccharides are macrobiomolecules formed by the polymerisation of monosaccharides.
In a polysaccharide chain ( say glycogen), the right end is called reducing end and left end is
called non- reducing end.
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Types of Polysaccharide :
1) Based on mono units:
a) Homopolysaccharide - Consist of a single monosaccharide unit. Eg : Cellulose
b) Heteropolysaccharide - Consist of more than one type of monosaccharide.
Eg : Hemi cellulose.
Cellulose
It is a structural and supporting polysaccharide
Cellulose is an unbranched homopolymer of glucose units, connected by

 1 - 4 glycosidic linkage.

It is the most abundant polysaccharide

Cellulose does not contain complex helices and hence cannot hold I2. Paper made from plant
pulp and cotton fibres is cellulose.
Chitin
Chitin is the second most abundant polysaccharide.
It is a structural polysaccharide present in the exoskeleton of Arthropods as well as present
in cell wall of fungus.
Chitin is an unbranched homopolymer of N - acetyl glucosamine.
Starch
Starch is the main storage polysaccharide of plants.
It is a homopolymer of glucose.
Starch exists in 2 forms. Amylose and Amylopectin
Amylose is the unbranched glucose chains present in starch.
Secondary form of amylose can change iodine in to deep blue colour.
Amylopectins are branched chains of glucose.

Glycogen
Glycogen is a highly branched homopolymer of glucose.

It is a storage polysaccharide in animals ( animal starch )

The glucose units are connected by  1 - 4 and  1 - 6 glycosidic linkage

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Inulin
Inulin is an unbranched homopolymer of fructose

Amino acids

Amino acids are substituted methanes.

Each amino acid is amphoteric due to the presence of basic amino group (- NH2) and acidic
carboxylic group (- COOH ). Amino acids contain an amino group and acidic group as
substituents on the same carbon i.e.   carbon. Hence they are called   amino acids.


H2 N C COOH

R
 - Amino acid

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Properties of Amino acids.

1) The chemical and physical properties of amino acids are essentially of the amino, carboxyl
and R- funtional groups.

2) A particular property of amino acids is the ionizable nature of -NH2 and -COOH groups.
Hence in solutions of different pH, the structure of amino acids changes.

+ +
H3N CH COOH H3N CH COO H2N CH COO

R R R
(A) (B) (C)

(Acidic medium) (Isoelectric medium) (Alkaline medium)

B is called Zwitterionic form.

Generally 20 proteinacious amino acids present in the nature known as standard amino acids.

Classification of Aminoacids

Based on number of amino and carboxylic groups there are neutral, acidic and basic amino
acids.

1) Neutral amino acids : Glycine, Alanine, Valine , Leucine

Glycine Alanine
H 2N CH COOH H 2N CH COOH
H
CH3

2) Acidic amino acids: Glutamic acid, Aspartic acid

3) Basic amino acids : Lysine, Arginine

4) Sulphur containing amnino acids - Cysteine and Methionine

5) Hydroxy Amino acids

Serine and Threonine have hydroxyl group ( -OH )in the side chain

H2 N CH COOH

CH2OH (Serine)

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6) Aromatic Aminoacids

Phenyl alanine, Tyrosine and Tryptophan have heterocyclic compounds in the side
chain. They are aromatic amino acids.

PROTEINS
Proteins are organic biomolecules formed from C,H,O,N and S. These are the most abundant
and most diverse organic compounds.

Most abundant protein in the Biosphere is RuBisCO

Collagen is the most abundant animal protein

Proteins are macromolecules and hetero polymers of amino acids.

Proteins are the polymers of amino acids, which are synthesized in ribosomes. There are four
structural levels in proteins.

1. Primary structure:

It is a linear chain of amino acids, called polypeptide. The amino acids are connected by
peptide bond. For peptide bond the first amino acid provides the -COOH group and the
second one provides -NH2 group. The left end of polypeptde is the N - terminal and right end
is the C - terminal. Primary structure is unstable.

2. Secondary structure:

It is more stable than primary structure due to the presence of additional hydrogen bonds.
These bonds formed between oxgen of -COOH group and hydrogen of -NH2 group.

 - helix - intra hydrogen bonding in a polypeptide leads to its right handed twist. It becomes
an  - helical protein. eg:  - Keratin present in hair and nails.

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 - pleated - Inter hydrogen bonding between two or more polypeptides leads to  - pleated
structure. eg:  - keratin in feathers and fibroin (natural silk )

Note : The most abundant animal protein collagen has triple helical structure. It is expaind
by the Indian Biologist G.N.Ramachandran.

3.Tertiary structure:

It is the maximum coiled form of a polypeptide. Tertiary proteins are stable due to the presence
of five type bonds

Peptide bonds, hydrogen bonds, ionic bonds, disulphide bonds and hydrophobic
bonds

Peptide and disulphide bonds are stronger than the other three ;

All enzymes have tertiary structure because it is the most reactive form of protein

eg: Myoglobin, enzymes

4. Quarternary structure :

It the most stable structure of proteins.

More than one polypeptides present in these proteins.

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eg: Haemoglobin - Adult haemoglobin consist of 4 subunits - 2 identical to each other

(2 subunits of   type and 2 subunits of   type)

Types of protein
On the basis of their constitution, proteins are classified in to two main groups

1. Simple proteins:

The protein contains only amino acids.

2. Conjugated proteins:

The protein has amino acids and non- protein groups.

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LIPIDS
The organic biomolecules formed from C, H and O. Oxygen is less than Carbon and Hydrogen
in number. Lipids are insoluble in polar solvents. They have low density and low melting
point.
Lipids are esters of glycerol and fatty acids.
Glycerol
Glycerol is a tryhydroxy propane.

CH2 OH

CH OH

CH2 OH

Fatty Acid
Fatty acids are hydrocarbons with a carboxylic group. If all Carbon atoms are connected by
single bonds the fatty acid becomes saturated.

eg: Palmitic acid (16 C) CH3 (CH2)14 COOH

Stearic acid (18 C ) CH3 (CH2)16 COOH

In unsaturated fatty acids one or more double bonds present among the Carbon atoms.
eg: Arachidonic acid (20- C containing)
Note : Unsaturated fatty acids have a low melting point than saturated fatty acids.
Melting point & stability are inversely proportional to the number of double bonds.
Classification of lipids
 Simple lipids
The lipid molecule contains only glycerol and fatty acids. Fatty acids (saturated or unsaturated)
combines with a glycerol in simple lipid.

Eg : Triglyceride

O CH2 O C R1

R2 C O CH O

CH2 O C R3

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Glycerol and fatty acids connected by ester bonds (each bond can release H2O)

 Compound lipids

Lipid molecules formed from glycerol, 2 fatty acids and an additional molecule.

In phospholipids phosphate group present as the third molecule.

Phospholipids are amphipathic due to the polar head and non - polar tails. They act as the
main structural component of plasma membrane.

Lecithin is a type of phospholipids. Lecithin present on alveoli act as a surfactant (reduces

surface tension)

 Derived Lipids

Sterols : The derived lipid contains hydrocarbon rings and hydrocarbon chains.

Cholesterol is the major form of sterol in animals.

It is essential for the stability and permeability of plasma membrane.

Steroid hormones and bile salts are synthesized from cholesterol.

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NUCLEIC ACIDS
The macro biomolecules formed from C, H, O, N & P.

DNA and RNA are two forms of nucleic acids which related to heredity and variations.
Nucleic acids are hetero polymers of nucleotides. Each nucleotide formed from pentose
sugar, nitrogen base and phosphate group .

The sugar is ribose or 2' deoxyribose

Nitrogen bases are heterocyclic nitrogen compounds. Double cyclic compounds are purines
and single ring compounds are pyrimidines.

Purines are two types

Adenine Guanine

Pyrimidines are three types

Cytosine Uracil Thymine
(5 methyl uracil)

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Phosphate group ( from phosphoric acid)

Nucleoside
The organic molecule formed from pentose sugar and nitrogen base.
Nitrogen base connected to the first carbon of sugar by  N - glycosidic bond.
RNA DNA
Ribose + adenine - Adenosine Deoxy ribose + adenine - Deoxy adenosine
Ribose + guanine - Guanosine Deoxy ribose + Guanosine - Deoxy guanosine
Ribose + cytosine - Cytidine Deoxy ribose + cytosine - Deoxy cytidine
Ribose + uracil - Uridine Deoxy ribose + thymine - Deoxy thymidine
Nucleotide

Nucleotide
The monomer of nucleic acid formed from nucleoside and phosphate group.
Phosphate group connected to the 5th carbon of sugar by phosphoester linkage.

Adenylic acid

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RNA Nucleotide

Adenosine + phosphate - Adenylic acid or adenosine mono phosphate (AMP)

Guanosine + phosphate - Guanylic acid or guanosine mono phosphate (GMP)

Cytosine + phosphate - Cytidylic acid or cytidine mono phosphate (CMP)

Uridine + phosphate - Uridylic acid or uridine mono phosphate (UMP)

DNA

Deoxy adenosine + phosphate - d adenylic acid or d adenosine mono phosphate (dAMP)

Deoxy guanosine + phosphate - d guanylic acid or d guanosine mono phosphate (dGMP)

Deoxy cytidine + phosphate - d cytidylic acid or d cytidine mono phosphate (dCMP)

Deoxy thymidine + phosphate - d thymidylic acid or d thymidine mono phosphate (dTMP)

Structure of DNA

James Watson & Francis Crick proposed the double helical structure of DNA.

Two strands of DNA are made up of sugar and phosphate groups. Nitrogen bases present
inside the strands. The strands are anti parallel .

Nucleotides of each strand are linked by phospho diester bonds.

Both strands of DNA are interconnected by the nitrogen base pairs. The pairing by hydrogen
bonds (A T, G C). Adenine pairs with thymine through 2 hydrogen bonds whereas
Guanine and Cytosine pairs through 3 hydrogen bonds.

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The base pairing and right hand twist gives a twisted ladder shape.

Part of DNA with a complete twist is a pitch of DNA.

The pitch has 360o angle of turn and 10 base pairs.

The ascent angle between two base pairs is 36o .

o o
Distance between two adjacent base pairs is 3.4 A . So the length of pitch is 34 A .

o
The width (distance between DNA strands) is 20 A .

CONCEPT OF METABOLISM

The biomolecules keep changing from one form to the other form, called the turn over

It takes place through metabolism, which is the sum total of all biochemical reactions that occur
within the cell.

The product formed in each step of metabolism is a metabolite.

The metabolic pathways are similar to the automobile traffic in a city.

This interlinked metabolic traffic is called the dynamic state of body constituents.

Every metabolic reaction is catalysed by the biocatalysts called enzymes.

Anabolism and Catabolism are two metabolic pathways.

Anabolism is the biosynthetic pathway (synthesis of complex compounds from simple substances)
eg: Protein synthesis , starch synthesis.

Catabolism is the degradation pathway (conversion of complex molecules in to simple products)

eg: Glycolysis , breakdown of muscle protein.

The energy liberated during degradation is stored in the form of chemical bonds in ATP molecules
(energy currency)

THE LIVING STATE

There is a number of biochemical reactions in living cells.

These reactions have the tendency to proceed towards a state of equilibrium.

The steady state of cell is in a non equilibrium state, which has a metabolic flux.

So living state is a non - equilibrium steady state to be able to perform work.

Living process is a constant effort to prevent falling in to equilibrium.

When a living system reach in equilibrium, it stops all metabolism and becomes dead.
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ENZYMES
Enzymes are biological catalysts because they can speed up the rate of metabolism.
Most of the enzymes are derivatives of tertiary proteins.
Sometimes nucleic acids behave like enzymes called ribozyme (23S rRNA)
Simple enzymes have a protein part only eg: pepsin
Conjugated enzymes have a protein part (apo enzyme ) and a non protein (co - factor)
Functional enzyme (Holo enzyme) = apo enzyme + co- factor
Co- factors are three types
1. Co- enzyme : An organic compound loosely attached to the apo enzyme . Most of the
co-enzymes are vitamin derivatives. eg: NAD, FAD, NADP, FMN,
2. Prosthetic group: A non protein tightly bounded to the apo enzyme. It may be organic or inorganic.
eg: Heam is prosthetic group of catalase & peroxydase
3. Activator : The metal ions loosely attached to the apo enzyme
eg: Zn - Carbonic anhydrase, Carboxy peptidase,
Alcohol dehydrogenase
Properties of enzymes
Enzymes are highly specific to their substrate and reaction.
Enzymes are highly sensitive to temperature and pH variations.
Each enzyme has an optimum temperature and pH for its maximum action.
Below 0o C enzyme becomes inactive and above 80o C they get denatured.
The change in rate of enzyme action due to the variation in 10o C within optimum range is the
temperature coefficient ( Q10 value ). For most of the enzymes it is 2.
The graph of temperature or pH relation with speed of enzyme action has parabolic shape.
Substrate concentration has a great influence in the rate of enzyme action.
In the beginning both are directly proportional. But after a limit substrate concentration has no effect
in the rate of enzyme. This limit is known as Vmax.
The substrate concentration required for 1/2 Vmax is called Km constant (Michaelis constant). It is
a measure of enzyme’s affinity to the substrate.

1
Km constant α =
affinity to the substrate

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The number of substrate molecules converted in to product by an enzyme per unit time is known
as the turn over number (TON) (Kcat)

TON  efficiency of enzyme

The turn over number is maximum for carbonic anhydrase.

It is 360 lakh/min or 6 lakh/sec.

Role of enzyme in a reaction

All biochemical reactions have a potential energy barrier.

The substrate must overcome this barrier to complete the reaction.

The substrate molecules with sufficient energy collides and can reach in a high energy transition
state. By the release of energy the transition state becomes product.

An enzyme can lower the level of activation energy. So the reaction attains transition state
(enzyme substrate complex) in a short period. It speed up the rate of reaction.

The difference in the energy of substrate and product is the energy of reaction.

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Enzyme inhibition
Any obstruction in enzyme action is an enzyme inhibition. Based on the nature of inhibitor
inhibitions are three types.

1. Competitive inhibition:

The inhibitor is structural analogue of substrate. There is competition between substrate

and inhibitor for the active site. It reduces the affinity of enzyme towards the substrate. This type
of inhibition is reversible . It can increase the Km value without changing Vmax.

eg: Malonic acid ( malonate ) is a competitive inhibitor of succinate dehydrogenase.

Classification of enzymes
On the basis of reaction they performed, enzymes are classified in to six major groups. The
classification was done by IUB (nternational Union for Biochemistry)

1. Oxido reductase : Catalyse oxidation and reduction reactions. These are the most abundant
form of enzyme.

S oxidised + S’ reduced S reduced + S’ oxidised

2. Transferase : Catalyse the transfer of a group from one substrate to another

S - G + S’ S + S’ - G

3. Hydrolases : Catalyse the hydrolytic breakdown of complex sustrate. All digestive

enzymes are hydrolases.

4. Lyases : Induce the cleavage without hydrolysis and addition of double bonds.

X Y

C C C C + X Y

5. Isomerase : Catalyse the rearrangement of molecular structure and formation of isomer.

6. Ligase : Catalyse the formation of linkage or bonds

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