CHAPTER - BIOMOLECULES

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PRIMARY METABOLITES: sugars, amino acids, lipids, nucleosides, nucleo2des, etc.

v rubber, essen2al oils, an2bio2cs, coloured
SECONDARY METABOLITES: alkaloids, flavonoids,
pigments, scents, gums, spices→ role in physiology not known→ have ecological importance

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1
 PROTEINS: heteropolymer→ amino acids linked by pep$de bond→ 20 amino acids
→Func2ons: structure (collagen), enzyme, immunity (an2body), hormone (insulin)
→Most abundant protein: in animal world – Collagen, in whole biosphere - Ribulose bisphosphate
Carboxylase-Oxygenase (RuBisCO)

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→ linear structure → protein threads are → 3-D structure → more than one
→ first amino acid: folded → important for polypep2de or subunits

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N-terminal amino acid → alpha-helix, biological ac$vi$es of → Haemoglobin
→ last amino acid: beta-pleated sheet proteins (2 ᾳ-chains, 2 β-chains)

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C-terminal amino acid

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POLYSACCHARIDES: long chains of sugars→ monosaccharides joined by glycosidic bond
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PURINES PYRIMIDINES RIBOSE 2’ DEOXYRIBOSE PHOSPHATE/

(dicyclic) (monocyclic) (RNA) (DNA) PHOSPHORIC ACID
Adenine Thymine
Guanine Cytosine
Uracil

Secondary structure of DNA (B-DNA): Watson-Crick model→ double helix→ an2parallel strands→
sugar-phosphate-sugar backbone→ A=T, G≡C→ 10 base pairs (one full turn of strand) → pitch (34Å) →
rise per base pair (3.4Å)

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ENZYMES: mostly proteins → ribozymes (nucleic acids) → ac$ve site (pocket of an enzyme where
substrate (S) fits in) → lowers ac2va2on energy, increases the rate of reac2on
o ENZYME ACTION: E + S ⇄ ES → EP → E + P, where, E-Enzyme, S-Substrate, P-Product

1. Temperature & Ph:

Highest ac2vity- op$mum
temperature, op$mum pH.
Enzymes denature at high
temperature.

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2. Concentra$on of substrate: At Vmax,
enzyme molecules are less than substrate

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molecules. Hence, binding stops.

Compe$$ve inhibi$on- Inhibitor

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competes with the substrate for the

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substrate-binding site due to its close
structural similarity → substrate cannot
gm bind → enzyme ac2on declines →
Eg. Inhibi2on of succinic dehydrogenase
by malonate
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o NOMENCLATURE OF ENZYMES:
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Oxidoreductases/ Oxidoreduc$on
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dehydrogenases (S reduced + S’ oxidised→ S oxidised + S’ reduced)

Transferases Transfer of a group, G (other than hydrogen)
(S – G + S’→ S + S’ – G)
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Hydrolases Hydrolysis of ester, ether, pep2de, glycosidic, C-C, C-halide, P-N bonds
Lyases Removal of groups (by mechanism other than hydrolysis, leaves double
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bonds)
Isomerases Interconversion of op$cal, geometric, posi$onal isomers
Ligases Links together 2 compounds (C-O, C-S, C-N, P-O bonds)
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o CO-FACTORS:
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 BIOMOLECULES
PREVIOUS YEAR QUESTIONS
NEET 2022
1. Read the following statements on lipids and find out correct set of statements:
(a) Lecithin found in the plasma membrane is a glycolipid
(b) Saturated fatty acids possess one or more c = c bonds
(c) Gingely oil has lower melting point, hence remains as oil in winter
(d) Lipids are generally insoluble in water but soluble in some organic solvents
(e) When fatty acid is esterified with glycerol, monoglycerides are formed
Choose the correct answer from the option given below:

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(1) (a), (b) and (c) only
(2) (a), (d) and (e) only

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(3) (c), (d) and (e) only
(4) (a), (b) and (d) only
Answer: (3) (c), (d) and (e) only are correct.

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Lecithin found in the plasma membrane is a phospholipid.

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Unsaturated fatty acids possess one or more c = c bonds.
11th NCERT, Page No. 144

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2. A dehydration reaction links two glucose molecules to produce maltose. If the formula for glucose is
C6H12O6 then what is the formula for maltose?
(1) C12H20O10
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(2) C12H24O12
(3) C12H22O11
(4) C12H24O11
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Answer: (3) C12H22O11

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11th NCERT, Page No. 151 (concept)

3. Match List-I with List-II

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List-I List-II
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(Biological Molecules) (Biological functions)

(a) Glycogen (i) Hormone

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(b) Globulin (ii) Biocatalyst

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(c) Steroids (iii) Antibody

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(d) Thrombin (iv) Storage product

Choose the correct answer from the options given below:

(1) (a) - (iii), (b) - (ii), (c) - (iv), (d) - (i)
(2) (a) - (iv), (b) - (ii), (c) - (i), (d) - (iii)
(3) (a) - (ii), (b) - (iv), (c) - (iii), (d) - (i)
(4) (a) - (iv), (b) - (iii), (c) - (i), (d) - (ii)
Answer: (4) (a) - (iv), (b) - (iii), (c) - (i), (d) - (ii)
11th NCERT, Page No. 147, 148

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 NEET 2021
1. Which of the following are not secondary metabolites in plants?
(1) Vinblastin, curcumin
(2) Rubber, gums
(3) Morphine, codeine
(4) Amino acids, glucose
Answer: (4)
Amino acids, glucose are primary metabolites.
11th NCERT, Page No. 146

2. Match list I with list II.

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List-I List-II

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(a) Protein (i) C=C double bonds

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(b) Unsaturated fatty acid (ii) Phosphodiester bonds

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(c) Nucleic acid (iii) Glycosidic bonds

(d) Polysaccharide (iv) Peptide bonds

Choose the correct answer from the options given below:
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(1) (a)-(ii); (b)-(i); (c)-(iv); (d)-(iii)
(2) (a)-(iv); (b)-(iii); (c)-(i); (d)-(ii)
(3) (a)-(iv); (b)-(i); (c)-(ii); (d)-(iii)
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(4) (a)-(i); (b)-(iv); (c)-(iii); (d)-(ii)

Answer: (3) (a)-(iv); (b)-(i); (c)-(ii); (d)-(iii)
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11th NCERT, Page No. 144, 151

3. Identify the incorrect pair.

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(1) Lectins - Concanavalin A

(2) Drugs - Ricin
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(3) Alkaloids - Codeine

(4) Toxin - Abrin
Answer: (2) Drugs - Ricin
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11th NCERT, Page No. 146

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4. Following are the statements with reference to 'lipids'.

(a) Lipids having only single bonds are called unsaturated fatty acids.
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(b) Lecithin is a phospholipid.

(c) Trihydroxy propane is glycerol.
(d) Palmitic acid has 20 carbon atoms including carboxyl carbon.
(e) Arachidonic acid has 16 carbon atoms.
Choose the correct answer from the options given below:
(1) (b) and (c) only
(2) (b) and (e) only
(3) (a) and (b) only
(4) (c) and (d) only
Answer: (1) (b) and (c) only Lipids having only single bonds are called saturated fatty acids.
Palmitic acid has 16 carbon atoms including carboxyl carbon.
Arachidonic acid has 16 carbon atoms.
11th NCERT, Page No. 14

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 NEET 2020
1. Identify the basic amino acid from the following:
(1) Lysine
(2) Valine
(3) Tyrosine
(4) Glutamic Acid
Answer: (1) Lysine
11th NCERT, Page No. 144

2. Which one of the following is the most abundant protein in the animals?
(1) Lectin

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(2) Insulin
(3) Haemoglobin

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(4) Collagen
Answer: (4) Collagen
11th NCERT, Page No. 148

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3. Match the following:

(a) Inhibitor of catalytic activity (i) Ricin

(b) Possess peptide bonds (ii) Malonate

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(c) Cell wall material in fungi (iii) Chitin

(d) Secondary metabolite (iv) Collagen

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Choose the correct option from the following:

(1) (a)-(iii), (b)-(i), (c)-(iv), (d)-(ii)
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(2) (a)-(ii), (b)-(iv), (c)-(iii), (d)-(i)

(3) (a)-(ii), (b)-(iii), (c)-(i), (d)-(iv)
(4) (a)-(iii), (b)-(iv), (c)-(i), (d)-(ii)
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Answer: (2) (a)-(ii), (b)-(iv), (c)-(iii), (d)-(i)

11th NCERT, Page No. 146, 147, 149, 158
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4. Identify the substances having glycosidic bond and peptide bond, respectively in their structure:
(1) Cellulose, lecithin
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(2) Inulin, insulin

(3) Chitin, cholesterol
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(4) Glycerol, trypsin

Answer: (2) Inulin, insulin
Inulin is a polymer of fructose, therefore, glycosidic bond.
Insulin is a proteinaceous hormone; therefore, it is made up of peptide bonds.
11th NCERT, Page No. 147, 148

5. Which of the following statements is correct?

(1) Adenine pairs with thymine through two H-bonds.
(2) Adenine pairs with thymine through one H-bond.
(3) Adenine pairs with thymine through three H-bonds.
(4) Adenine does not pair with thymine.
Answer: (1) Adenine pairs with thymine through two H-bonds.
11th NCERT, Page No. 152

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 NEET 2019
1. Concanavalin A is:
(1) an alkaloid
(2) an essential oil
(3) a lectin
(4) a pigment
Answer: (3) a lectin
11th NCERT, Page No. 146

2. Consider the following statements:

(A) Coenzyme or metal ion that is tightly bound to enzyme protein is called prosthetic group.

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(B) A complete catalytic active enzyme with its bound prosthetic group is called apoenzyme.
Select the correct option:

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(1) Both (A) and (B) are true.
(2) (A) is true but (B) is false.
(3) Both (A) and (B) are false.

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(4) (A) is false but (B) is true.

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Answer: (3) Both (A) and (B) are false.
11th NCERT, Page No. 159

3. Purines found both in DNA and RNA are:

(1) Adenine and thymine
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(2) Adenine and guanine
(3) Guanine and cytosine
(4) Cytosine and thymine
Answer: (2) Adenine and guanine
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11th NCERT, Page No. 149

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4. Which of the following glucose transporters is insulin-dependent?

(1) GLUT I
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(2) GLUT II
(3) GLUT III
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(4) GLUT IV
Answer: (4) GLUT IV
11th NCERT, Page No. 147
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 IMPORTANT MCQs
1. Given below are two statements:
Statement I:
Proteins, nucleic acids and polysaccharides are polymeric macromolecules found in the acid
insoluble fraction.
Statement II:
Lipids are present in the acid soluble fraction as their molecular weight do not exceed 800 Da.
In the light of the given statements, choose the correct answer from the options given below:
(1) Statement I is incorrect but Statement II is correct
(2) Both Statement I and Statement II are correct

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(3) Both Statement I and Statement II are incorrect
(4) Statement I is correct but Statement II is incorrect

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Solution:
11th NCERT, Page No. 146

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Correct answer: (4) Statement I is correct but Statement II is incorrect

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• Lipids are present in the acid insoluble fraction even though their molecular weight do not
exceed 800 Da.

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• On grinding a tissue, when the cell membrane disrupts, lipids form vesicles which are not
water soluble and get separated along with the acid insoluble fraction.
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2. Which of the following statement about ‘amino acids’ is incorrect?
(1) They are substituted methane.
(2) In serine, the ‘R’ group consists of a hydroxy methyl group.
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(3) As tryptophan is an aromatic amino acid, it cannot exist in the zwitterionic form.
(4) Glycine is the simplest amino acid.
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Solution:
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11th NCERT, Page No. 144

Correct answer: (3) is incorrect
• All amino acids can exist in zwitterionic form (ionizable nature of -NH2 and COOH).
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3. Given below are two statements: one is labelled as Asser-on (A) and the other is labelled as
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Reason (R).
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Assertion (A): The living state is a non-equilibrium steady state to be able to perform work.
Reason (R): Systems at equilibrium cannot perform work.
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In the light of the given statements, choose the correct answer from the options given below:
(1) (A) is not correct but (R) is correct
(2) Both (A) and (R) are correct and (R) is the correct explanation of (A)
(3) Both (A) and (R) are correct but (R) is not the correct explanation of (A)
(4) (A) is correct but (R) is not correct

Solution:
11th NCERT, Page No. 153
Correct answer: (2) Both (A) and (R) are correct and (R) is the correct explanation of (A)

4. Match the column I with column II and select the correct answer from the codes given below:

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 Column I Column II
1. Abrin a. Pigment
2. Codeine b. Drug
3. Anthocyanins c. Alkaloid
4. Curcumin d. Terpenoids
5. Diterpenes e. Toxin

(1) 1-e, 2-c, 3-a, 4-b, 5-d

(2) 1-c, 2-e, 3-b, 4-a, 5-d

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(3) 1-b, 2-c, 3-e, 4-a, 5-d
(4) 1-e, 2-a, 3-b, 4-c, 5-d

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Solution:

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11th NCERT, Page No. 146

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Correct answer: (1) 1-e, 2-c, 3-a, 4-b, 5-d

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5. Which of the following statements related to ‘biomolecules’ are correct?
(a) All the carbon compounds present in the living tissues can be called biomolecules.
(b) Nucleosides are the building blocks for nucleic acids.
(c) ‘GLUT-4’ is a protein which enables glucose transport into cells.
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(d) Glucose is a 6-carbon aldose sugar.

(1) only (b), (d)

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(2) only (a), (c) and (d)

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(3) only (a), (b) and (d)

(4) only (a), (c)
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Solution:
11th NCERT, Page No. 143, 145, 147, 149
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Correct answer: (2) only (a), (c) and (d) are correct
• Statement (b) is incorrect.
• Nucleotides are the building blocks for nucleic acids.
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6. Given below are two statements:

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Statement I: Arachidonic acid has 16 carbon atoms including the carboxyl carbon.
Statement II: A fatty acid has a carboxyl group attached to an R group ( methyl (–CH3), or ethyl (–
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C2H5).
In the light of the given statements, choose the correct answer from the options given below:
(1) Statement I is incorrect but Statement II is correct
(2) Both Statement I and Statement II are correct
(3) Both Statement I and Statement II are incorrect
(4) Statement I is correct but Statement II is incorrect

Solution:
11th NCERT, Page No. 144
Correct answer: (1) Statement I is incorrect but Statement II is correct
• Arachidonic acid has 20 carbon atoms including the carboxyl carbon.

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7. Identify the correct statement about proteins:
(1) Proline is a heteropolymer.
(2) In proteins, both left and right-handed helices are observed.
(3) The amino (-NH2) group of two amino acids form the peptide bond.
(4) The tertiary structure of proteins involves the formation of hydrogen and disulphide bonds.

Solution:
11th NCERT, Page No. 147, 150, 151
Correct answer: (4) is correct

8. Given below are two statements: one is labelled as Asser-on (A) and the other is labelled as
Reason (R).

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Assertion (A): Cholesterol synthesis from acetic acid in our body is an example of a biosynthetic

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pathway.
Reason (R): Anabolic pathways consumes energy and leads to the formation of a complex structure

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from a simple structure.
In the light of the given statements, choose the correct answer from the options given below:

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(1) (A) is not correct but (R) is correct
(2) Both (A) and (R) are correct and (R) is the correct explanation of (A)

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(3) Both (A) and (R) are correct but (R) is not the correct explanation of (A)
(4) (A) is correct but (R) is not correct
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Solution:
11th NCERT, Page No. 153
Correct answer: (2) Both (A) and (R) are correct and (R) is the correct explanation of (A)
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9. Which of the following statement regarding polysaccharides is false?

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(1) N-acetyl galactosamine is a chemically modified sugar.

(2) Paper made from plant pulp and cotton fibre is cellulosic.
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(3) The cellulose-I2 complex is blue in colour.

(4) Inulin is a polymer of fructose.
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Solution:
11th NCERT, Page No. 148, 149
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Correct answer: (3) is false.

• Cellulose does not contain complex helices and hence cannot hold I2.
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10. Match the column I with column II and select the correct answer from the codes given below:
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Column I Column II
(Component) (% of the total
cellular mass)
1. Proteins a. 70-90
2. Water b. 2
3. Carbohydrates c. 5-7
4. Nucleic acids d. 10-15
5. Lipids e. 3

(1) 1-d, 2-a, 3-c, 4-b, 5-e

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(2) 1-c, 2-a, 3-b, 4-d, 5-e
(3) 1-c, 2-a, 3-b, 4-e, 5-d
(4) 1-d, 2-a, 3-e, 4-c, 5-b

Solution:
11th NCERT, Page No. 147
Correct answer: (4) 1-d, 2-a, 3-e, 4-c, 5-b

11. Which of the following statement about enzymes is incorrect?

(1) The binding of the substrate with the enzyme, induces the enzyme to alter its shape.
(2) Enzymes isolated from thermophilic organisms retain their catalytic power even at high

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temperatures.
(3) Low temperature preserves the enzyme in a temporarily inactive state.

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(4) Catalytic activity is retained even when the co-factor is removed from the enzyme.

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Solution:
11th NCERT, Page No. 154, 157, 159

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Correct answer: (4) is incorrect
• Catalytic activity is lost when the co-factor is removed from the enzyme.

12. Given below are two statements:

Statement I:
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Co-factors which bind to the enzyme are also known as apoenzyme.
Statement II:
Co-factors bind to the enzyme to make them catalytically active.
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In the light of the given statements, choose the correct answer from the options given below:
(1) Statement I is incorrect but Statement II is correct
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(2) Both Statement I and Statement II are correct

(3) Both Statement I and Statement II are incorrect
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(4) Statement I is correct but Statement II is incorrect

Solution:
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11th NCERT, Page No. 159

Correct answer: (1) Statement I is incorrect but Statement II is correct
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• When co-factors bind to the enzyme, the protein portion of the enzymes is called the
apoenzyme.
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13. Given below are two statements: one is labelled as Asser-on (A) and the other is labelled as
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Reason (R).

Assertion (A): The two adjacent monosaccharides in a polysaccharide are linked by a glycosidic
bond.
Reason (R): The glycosidic bond formation does not involve the elimination of a water moiety.
In the light of the given statements, choose the correct answer from the options given below:
(1) (A) is not correct but (R) is correct
(2) Both (A) and (R) are correct and (R) is the correct explanation of (A)
(3) Both (A) and (R) are correct but (R) is not the correct explanation of (A)
(4) (A) is correct but (R) is not correct

Solution:
11th NCERT, Page No. 151

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Correct answer: (4) (A) is correct but (R) is not correct
• Glycosidic bond is formed by dehydration.

14. Given below are two statements: one is labelled as Asser-on (A) and the other is labelled as
Reason (R).

Assertion (A): In our skeletal muscle, under anaerobic conditions, glucose is converted into lactic
acid while under normal aerobic conditions, glucose is completely oxidised .
Reason (R): A metabolic pathway can lead to the formation of different products in different
conditions.

In the light of the given statements, choose the correct answer from the options given below:

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(1) (A) is not correct but (R) is correct
(2) Both (A) and (R) are correct and (R) is the correct explanation of (A)

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(3) Both (A) and (R) are correct but (R) is not the correct explanation of (A)
(4) (A) is correct but (R) is not correct

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Solution:

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11th NCERT, Page No. 155
Correct answer: (2) Both (A) and (R) are correct and (R) is the correct explanation of (A)

15. Given below are two statements:

Statement I:
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In a nucleic acid, a phosphate moiety links the 3’-carbon of one sugar of one nucleotide to the 5’-
carbon of the sugar of the succeeding nucleotide.
Statement II:
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The bond between the phosphate and hydroxyl group of sugar is an ester bond.
In the light of the given statements, choose the correct answer from the options given below:
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(1) Statement I is incorrect but Statement II is correct

(2) Both Statement I and Statement II are correct
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(3) Both Statement I and Statement II are incorrect

(4) Statement I is correct but Statement II is incorrect
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Solution:
11th NCERT, Page No. 151
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Correct answer: (2) Both Statement I and Statement II are correct

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NEET 2023
Key Notes on
BIOMOLECULES
Covering 2 to 4 MCQs in NEET
Biomentors Classes Online, Mumbai
© All right reserved
Copyright – Biomentors
1. Trichloroacetic acid (Cl3CCOOH) à
Used to analyse chemical composition of living
tissue
Acid-soluble pool à
Compounds found have molecular weights
ranging from 18 to around 800 daltons (Da)
approximately. @ Micro molecules
Retentate or the acid-insoluble fraction à
Only four types of organic compounds i.e.,
proteins, nucleic acids, polysaccharides and
lipids. @ Macro molecules except Lipid
Except lipids, all have molecular weights
10000 daltons and above.
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2. All the carbon compounds present in living tissues
à ‘Biomolecules’.
3. Amino acids à
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Organic compounds
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Have an amino group and an acidic group on
the same carbon i.e., the alpha-carbon. Hence,
they are called α-amino acids.
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They are substituted methanes.
There are four substituent groups
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Hydrogen, Carboxyl group, Amino group and A
variable group designated as R group.
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Based on the nature of R group there are many
amino acids.
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In proteins à only of 20 types of amino acids .
The R group à
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The chemical and physical properties of amino
acids determined by à Amino group,
carboxyl group and the R functional groups.
Based on number of amino & carboxyl groups,
o Acidic (e.g., glutamic acid),
o Basic (lysine) and
o Neutral (valine) amino acids.
Aromatic amino acids (tyrosine,
o
phenylalanine, tryptophan).
o A particular property of amino acids is
the ionizable nature of –NH2 and –
COOH groups. @ Isoelectric pH &
Zwittor ion
o In solutions of different pHs, the
structure of amino acids changes.
4. Lipids
o Generally water insoluble.
o A fatty acid has a carboxyl group attached to
an R group.
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o The R group à Generally 1 carbon to 19
co
carbons
o Palmitic acid has 16 carbons
o Arachidonic acid has 20 carbon atoms
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o Fatty acids
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§ Saturated (without double bond)
§ unsaturated (with one or more
gm C=C double bonds).
§ Most simple lipid is glycerol
which is trihydroxy propane.
o Many lipids have both glycerol and
fatty acids.
o Oils have lower melting point (e.g.,
gingely oil)
o Some lipids have phosphorous and a
phosphorylated organic compound
à Phospholipids à Found in cell
membrane.
§ Example - Lecithin
o Neural tissues have lipids with more
complex structures.
5. Nitrogen Base à
o Heterocyclic rings
o Nitrogen bases – adenine, guanine, cytosine,
uracil, and thymine.
o Nitrogen base + sugar àNucleosides.
o Adenosine, guanosine, thymidine, uridine
and cytidine are nucleosides.
o Nucleotide = Nucleoside +Phosphate
o Nucleotides à Adenylic acid, thymidylic acid,
guanylic acid, uridylic acid and cytidylic acid
o Nucleic acids like DNA and RNA consist of
nucleotides only.
o DNA & RNA à Genetic material.
6. PRIMARY AND SECONDARY METABOLITES
o Primary metabolites à Have identifiable
functions and play roles in normal
physiological processes.
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 § Proteins, amino acids, nucleotides,
carbohydrates, lipids etc.
o Secondary metabolites à Not clear
understanding about the role or functions of
all the ‘secondary metabolites’ in host
organisms.
§ Many useful to ‘human welfare’
§ Some secondary metabolites have
ecological importance.
§ e.g., rubber, drugs, spices, scents,
pigments, alkaloids, flavonoids, rubber,
essential oils, antibiotics, coloured
14. GLUT4 is the insulin-regulated glucose transporter
found primarily in adipose tissues and striated
muscle (skeletal and cardiac).
15. Collagen is the most abundant protein in animal
world
16. Ribulose bisphosphate Carboxylase-Oxygenase
(RuBisCO) is the most abundant protein in the
whole of the biosphere.
17. POLYSACCHARIDES
o Long chains of sugars.
o Threads containing different
monosaccharides as building blocks.

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pigments, scents, gums, spices. o cellulose (Polymer of beta-D-glucose) &
Pigments Carotenoids, Starch (Polymer of alpha-D-glucose)

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Anthocyanins, etc. 18. Cellulose is a homopolymer;
Alkaloids Morphine, Codeine Starch is à A store house of energy in plant

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Terpenoides Monoterpenes,Diterpenes
tissues;
Essential oils Lemon grass oil

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Glycogen is à A store house of energy in
Toxins Abrin, Ricin
animal tissue
Lectins Concanavalin A
Drugs
Polymers
Vinblastin, curcumin
Rubber, gums, cellulose gm
19. Inulin is a polymer of fructose.
20. In Glycogen à The right end is called the reducing
end and the left end is called the non-reducing end.
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7. PROTEINS 21. Starch forms helical secondary structures. Starch can
o Polypeptides. hold I2 molecules in the helical portion. The starch-I2
o Linear chains of amino acids linked by is blue in colour.
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peptide bonds 22. Cellulose does not contain complex helices and
hence cannot hold I2 .
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o Polymer of amino acids.

o 20 types of amino 23. Plant cell walls, Cotton fibre, Paper pulp are made of
o Heteropolymer and not a homopolymer. cellulose.
us

8. Dietary proteins are the source of essential amino 24. Complex polysaccharides à Have as building
acids. We get through our diet/food. blocks, amino-sugars and chemically modified
sugars (e.g., glucosamine, N-acetyl galactosamine,
ay

9. Proteins carry out many functions in living

organisms etc.).
Protein Functions o Exoskeletons of arthropods, (chitin)
ia

Collagen Intercellular ground substance o These complex polysaccharides are mostly

Trypsin Enzyme homopolymers. (2020 – NCERT)
in

Insulin Hormone 25. NUCLEIC ACIDS:

Antibody Fights infectious agents Polynucleotides.
sa

Receptor Sensory reception (smell, taste, Building block à nucleotide.

hormone, etc.)
GLUT -4 Enables glucose transport
into cells
10. GLUCOSE TRANSPORTERS are a group of membrane
proteins that facilitate the transport of glucose
across the plasma membrane.
11. The GLUT or SLC2A family are a protein family that is
found in most mammalian cells.
12. GLUT is a type of uniporter transporter protein.
13. Glucose transporter type 4 (GLUT-4) is a protein
encoded, in humans, by the SLC2A4 gene.
A nucleotide consist of à 3 components
1. N Base, 2. Pentose sugar 3. a phosphate.
Heterocyclic compounds in nucleic acids are
the nitrogenous bases à adenine, guanine,
uracil, cytosine, and thymine.
Adenine and Guanine are substituted purines
while the rest are substituted pyrimidines.
The sugar found in polynucleotides à either
ribose or 2’ deoxyribose.
A nucleic acid containing deoxyribose à DNA
A nucleic acid containing ribose à RNA

14
26. STRUCTURE OF PROTEINS
Biologists describe the protein structure at four
levels.
The sequence of amino acids à Primary
structure of a protein.
The first amino acid à N-terminal amino acid.
The last amino acid à C-terminal amino acid.
A protein thread is folded in the form of a helix
à Secondary structure
In proteins, only right handed helices are
observed.
In addition, the long protein chain is also
folded upon itself à Tertiary structure
This gives us a 3-dimensional view of a protein.
Tertiary structure is absolutely necessary for the
many biological activities of proteins.
Some proteins are an assembly of more than
one polypeptide or subunits. à quaternary
structure of a protein.
Adult human haemoglobin consists of 4
subunits. @ 2 Alpha & 2 Beta chains
27. NATURE OF BOND LINKING MONOMERS IN A
4@
POLYMER à
In a protein, amino acids are linked à
by peptide bond
8
In a polysaccharide monosaccharides are
linked à by glycosidic bond.
h2
In a nucleic acid nucleotides are linked à by
Phosphodiester bond
us
a phosphate moiety links the 3’-carbon of one sugar
of one nucleotide to the 5’-carbon of the sugar of the
succeeding nucleotide.
ay
28. Nucleic acids exhibit a wide variety of secondary
structures.
ia
Secondary structures exhibited by DNA is the
famous Watson-Crick model.
in
DNA is a double helix.
The two strands are antiparallel i.e., run in the
sa
opposite direction.
The backbone is formed by the sugar
phosphate-sugar chain.
A and G of one strand pairs with T and C, on the
other strand.
2 H - bonds between A and T and 3 H - bonds
between G and C.
Each strand appears like a helical staircase.
Each step of ascent à a pair of bases.
At each step of ascent, the strand turns 36°.
One full turn of the helical strand would
involve ten steps or ten base pairs.
The pitch would be 34Å. The rise per base pair
would be 3.4Å.
This form of DNA with the above mentioned
features is called B-DNA.
29. Biomolecules have a turn over.
o Constantly being changed into some other
biomolecules and also made from some
other biomolecules.
o Breaking and making is through chemical
reactions à metabolism.
o In other words, metabolites are converted
into each other in a series of linked reactions
m
called metabolic pathways.
o These metabolic reactions is that every
co
chemical reaction is a catalysed reaction.
o Proteins with catalytic power are named
l.
enzymes.
ai
30. Metabolic pathways can lead to
o More complex structure from a simpler
gm structure (biosynthetic or anabolic pathways)
o Simpler structure from a complex structure
(catabolic pathways)
o Anabolic pathways, as expected, consume
energy.
o catabolic pathways lead to the release of
energy.
o Energy currency in living systems is the bond
energy in a chemical called adenosine
triphosphate (ATP).
o ATP is energy currency of cell
31. These biomolecules are in a metabolic flux.
32. Any chemical or physical process moves
spontaneously to equilibrium.
33. The steady state is a non-equilibrium state.
34. The living state is a non-equilibrium steady-state to
be able to perform work
35. Living process is a constant effort to prevent falling
into equilibrium. This is achieved by energy input.
36. Metabolism provides a mechanism for the
production of energy. Hence the living state and
metabolism are synonymous.
37. ENZYMES
o Almost all enzymes are proteins.
o Ribozymes à catalytic RNA.
o An active site of an enzyme is a crevice or
pocket into which the substrate fits.
o Enzymes get damaged at high temperatures
(say above 40°C).
o Thermal stability seen in enzymes isolated
from thermophilic organisms.
15
38. Rate of a physical or chemical process refers to the
amount of product formed per unit time.
39. There are thousands of types of enzymes each
catalysing a unique chemical or metabolic reaction.
40. Enzymes eventually bring down activation energy
barrier making the transition of ‘S’ to ‘P’ more easy.
41. Each enzyme (E) has a substrate (S) binding site in
its molecule so that a highly reactive enzyme-
substrate complex (ES) is produced.
42. ES complex is short-lived and dissociates into its
product(s) P and the unchanged enzyme with an
intermediate formation of the enzyme-product
complex (EP).
43. The catalytic cycle of an enzyme action has following
steps:
o Active site of Enzyme + Substrate à Enzyme
substrate complex formation
o In ES complex the substrate ffitted more
tightly
o Enzyme- product complex is formed through
catalysis (Bond reorganisation)
o Dissociation of Enzyme Product complex into
4@
enzyme & product
44. Factors Affecting Enzyme Activity
o The activity of an enzyme can be affected by a
change in the conditions which can alter the
8
tertiary structure of the protein.
h2
o Temperature, pH, change in substrate
concentration or binding of specific chemicals
us
that regulate its activity.
o Enzymes generally function in a narrow range
of temperature and pH
ay
o Each enzyme shows its highest activity at a
particular temperature & pH called the
ia
optimum temperature & optimum pH.
o Activity declines both below and above the
in
optimum value.
o Low temperature preserves the enzyme in a
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temporarily inactive state
o high temperature destroys enzymatic activity
because proteins are denatured by heat.
45. Concentration of Substrate à
At fixed enzyme concentration with the
increase in substrate concentration à the
velocity of the enzymatic reaction rises at first.
à reaches a maximum velocity (Vmax) à not
exceeded by any further rise in concentration of
the substrate. à This is because no free
enzyme molecules to bind with the additional
substrate molecules @ SATURATION EFFECT
46. The Michaelis constant (KM) is defined as the
substrate concentration at which the reaction rate is
half of its maximal value (or in other words it
defines the substrate concentration at which half of
the active sites are occupied).
47. An enzyme with a high Km has a low affinity for its
substrate, and requires a greater concentration of
substrate to achieve Vmax
48. The activity of an enzyme is also sensitive to the
presence of specific chemicals that bind to the
enzyme. When the binding of the chemical shuts off
enzyme activity, the process is called inhibition and
m
the chemical is called an inhibitor.
49. When the inhibitor closely resembles the substrate
co
in its molecular structure and inhibits the activity of
the enzyme, it is known as competitive inhibitor.
l.
e.g., inhibition of succinic dehydrogenase by
ai
malonate which closely resembles the
substrate succinate in structure. Such
gm competitive inhibitors are often used in the
control of bacterial pathogens.
50. CLASSIFICATION & NOMENCLATURE OF ENZYMES
On the basis of the type of reactions à 6
classes each with 4-13 subclasses
Named accordingly by a four-digit number.
OXIDOREDUCTASES/DEHYDROGENASES:
Enzymes which catalyse oxidation-reduction
between two substrates
TRANSFERASES:
Enzymes catalysing a transfer of a group
HYDROLASES:
Enzymes catalysing hydrolysis of ester, ether,
peptide, glycosidic, C-C, C-halide or P-N bonds.
LYASES:
Enzymes that catalyse removal of groups from
substrates by mechanisms other than
hydrolysis leaving double bonds.
ISOMERASES:
Includes all enzymes catalysing inter-
conversion of optical, geometric or positional
isomers.
LIGASES:
Enzymes catalysing the linking together of 2
compounds, e.g., enzymes which catalyse
joining of C-O, C-S, C-N, P-O etc. bonds.
51. CO-FACTORS à
o Non-protein constituents
o bound to the enzyme to make the enzyme
catalytically active.
o In these instances, the protein portion of the
enzymes is called the APOENZYME.
16
 o Three kinds of cofactors may be identified:
§ prosthetic groups,
§ co-enzymes and
§ metal ions.
o Prosthetic groups are organic compounds à
tightly bound to the apoenzyme.
o Co-enzymes are also organic compounds à
their association with the apoenzyme is only
transient, usually occurring during the course
of catalysis.
o The essential chemical components of many
coenzymes are vitamins, e.g., coenzyme
nicotinamide adenine dinucleotide (NAD)
and NADP contain the vitamin niacin.
o A number of enzymes require metal ions for
their activity
e.g., zinc is a cofactor for the proteolytic
enzyme carboxypeptidase.
o Catalytic activity is lost when the co-factor is
removed from the enzyme which testifies that
they play a crucial role in the catalytic activity
of the enzyme.
4@
GOLDEN POINTS by BIOMENTORS from PYQs
1. Living organisms have more carbon, oxygen and
8
hydrogen per unit mass than inanimate objects
2. Silicon is not found in living organisms
h2
3. Amino acids have both an amino group and a carboxyl
group in their structure.
us
4. An amino acid under certain condition have both
positive and negative charges simultaneously in the
ay
same molecule. Such a form of amino acid is calledà
Zwitter ionic form
5. Fructose have the same number of carbon as present
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in glucose
6. An acid soluble compound formed by phosphorylation
in
of nucleoside is called à Nucleotide
7. When we homogenise any tissue in an acid the acid
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soluble pool represents Cytoplasm
8. The most abundant chemical in living organisms à
Water
9. Proteins are heteropolymers usually made of à20
types of monomers
10. Proteins perform many physiological functions. For
example some proteins function as enzymes & some
proteins performs as à Hormones
11. Glycogen is a homopolymer made up of Glucose units
12. The number of ‘ends’ in a glycogen molecule would be
à Equal to the number of branches plus one
13. The primary structure of a protein molecule has àTwo
ends
14. Dissolving CO2 in water reactions is also enzyme-
mediated in biological system
15. 80% of cytoplasm in plant cells is Water
16. Two groups of involved in peptide linkage between
different amino acids are NH2 & COOH
m
17. Role of enzyme in reactions is to àDecrease activation
energy
co
18. End product is responsible for inhibition of enzymatic
process during feed back.
l.
19. Enzymes are not found in à Viruses (except Retro
virus family)
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20. ATP is a nucleotide
21. Glycoproteins have carbohydrate as prosthetic group.
gm
22. Km value of enzyme is substrate conc. at 1/2 V max
23. Nitroginase Enzyme first used for nitrogen fixation
24. Most of the water in the young plant cell à in
cytoplasm; Mature plant cell à in Central vacuole
25. Osmotically inactive chief stored material in animal
body is Glycogen
26. Lipids are insoluble in water because lipid molecules
are à Hydrophobic
27. Galactose is a reducing sugar
28. Sucrose not give positive Fehling’s test (non reducing
sugar)
29. Mathematical explanation for enzyme action on
substrate was provided byà Michaelis and Menten
30. Km value is dependent upon Substrate concentration
31. The major role of minor elements inside living
organisms is to act as à Co-factors of enzymes
32. Tyrosinase needs copper as an activator
33. The catalytic efficiency of two different enzymes can be
compared by the Km value
34. Competitive inhibition is seen when the substrate and
the inhibitor compete for the active site on the
enzyme
35. Enzymes, vitamins and hormones can be classified
into a single category of biological chemicals, because
all of these help in regulating metabolism
36. Nucleotides are building blocks of nucleic acids.
37. Each nucleotide is a composite molecule formed by
Base-sugar-phosphate
38. Carbohydrates, the most abundant biomolecule on
earth, are produced by Some bacteria, algae and
green plant cells
39. The simplest amino acid is àGlycine
40. Richest source of protein is à Soyabean
41. This curves shows à
17
 A B C D
A = Normal enzyme action, Transition Potential Activation Activation
B = Competitive inhibition, state energy energy energy with
C = Non-competitive inhibition without enzyme

m
42. An organic substrate bound to an enzyme and enzyme
essential for its activity is calledà Coenzyme 62. A disaccharide that gives two molecules of glucose on

co
43. About 98 per cent of the mass of every living organism hydrolysis isà Maltose
is composed of just six elements including carbon, 63. The given curve shows enzymatic activity in relation to
hydrogen, nitrogen, oxygen and Phosphorus and temperature

l.
sulphur

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44. Boron element is very essential for uptake and
utilization of Ca2+ and membrane function.

gm
45. In a protein the amino acids are linked by Peptide
bonds
46. Three most abundant elements in protoplasm are
Carbon, hydrogen, oxygen X axis Y axis
4@
47. Chitin is present in the cell wall of fungi Temperature Enzyme activity
48. Carbohydrates are commonly found as starch in plant 64. The enzymes carries out the initial step in the
storage organs. digestion of milk in humans is Pepsin
49. A competitive inhibitor of succinic dehydrogenase is 65. In humans, milk protein-digesting enzyme is
8

àMalonate the stomach is pepsin. In calves it is rennin. Rennin is

h2

50. Inulin, a low molecular weight polysaccharide is also present in small amounts in human infants but
obtained from roots of à Dahlia ; polymer of D-
not adults.
fructose in which monomer units are linked together
us

66. Pepsin acts on water insoluble caseinogen (milk

by beta (1->2) glycosidic linkage.
51. Collagen is à Fibrous protein protein) to form soluble 'casein'.
52. Spirulina BGA is the rich source of à Protein 67. Lecithin is a component of cell membrane
ay

53. In human per cent of body weight of carbohydrates,

lipids and proteins respectively is à1, 15, 17
ia

54. Table sugar is Sucrose

55. In a disaccharide two monosaccharides are linked by a
in

glycosidic bond.
56. Excess carbohydrates and proteins are stores in the
body as Fats
sa

57. Cellulose is a homopolymer 68. Glycerol is a trihydroxy propane

58. Enzymes require optimum temperature & pH for 69. In a normal adult, ascending order of concentration of
maximal activity
following molecules is: K > Na > Fe > Cu
59. Enzymes are denatured at high temperature but in
70. A phosphoglyceride is always made up of saturated or
certain exceptional organisms they are effective even
at temperatures 80°-90℃ unsaturated fatty acids esterified to a glycerol
60. Enzymes are highly specific molecule to which a phosphate group is also attached
61. Remember the figure give below 71. Macromolecule chitin is nitrogen containing
polysaccharide
72. Transition state structure of the substrate formed
during an enzymatic reaction is à Transient and
unstable

18
73. The essential chemical components of many
coenzymes are Vitamins of B complex mainly
74. Enzymes are denatured at high temperatures
75. Substrate binds with enzyme at its active site
76. A non-competitive inhibitor binds the enzyme at a site
distinct from that which binds the substrate
77. Malonate is a competitive inhibitor of succinic
dehydrogenase
78. Sucrose is a non-reducing carbohydrate.
79. The presence of competitive inhibitor increases the Km
of the enzyme for the substrate
80. A competitive inhibitor reacts reversibly with the
enzyme to form an enzyme –inhibitor complex
81. In competitive inhibition, the inhibitor molecule is not
chemically changed by the enzyme
82. The competitive inhibitor does not effect the rate of
breakdown of the enzyme substrate complex
83. An allosteric inhibitor of the enzyme acts by binding to
the non-catalytic site of the enzyme (allosteric site)
84. The two polypeptide of human insulin are linked
together by à Disulphide bridges
85. Holoenzyme = Apoenzyme + Cofactor
4@
86. Cofactor à may be Prosthetic group, Co-enzymes or
Metal activator
87. The two functional groups characteristic of sugars are
8
Carbonyl and hydroxyl
h2
88. Term lipid was coined by Bloor (1943). These are esters
of fatty acids and alcohol.
us
89. Linoleic acid, linolenic acid, arachidonic acid are
essential fatty acid (Evans and Burr 1928).
90. Deficiency of essential fatty acid may cause follicular
ay
hyper keratosis disease.
91. Bees wax is a common example of wax. It is a
ia
combination of palmitic acid and mericyl alcohol
(C 30 H 61OH ) .
in
92. Phospholipids : It is amphipathic molecule. These
sa
contain phosphoric acid. It helps in transport,
metabolism, blood clotting and permeability of cell
membrane. e.g., Lecithin, cephalin
93. Biomarker of human faeces à Coprosterol ; It is
formed as a result of the reduction by bacteria in
intestine from the double bond of cholesterol between
C5 and C6.
94. Terpenes : found in essential oils and present mostly in
oils of camphor, eucalyptus, lemon and mint. Phytol is
a terpenoid alcohol present in Vitamin A, K, E and in
pigments like chlorophyll carotenoid.
95. Total known amino acid are more than 200 out of these
only 20 amino acid takes part in protein synthesis
called protein amino acid.
96. Glycine is a simplest amino acid.
97. Sulphur containing amino acids : They have sulphur
atom in side chain. e.g., methionine, cysteine.
98. Proline and hydroxyproline have, NH (imino group)
instead of NH 2 hence are called imino acids.
99. Purines : Purines are 9 membered double ringed
nitrogenous bases which possess nitrogen at 1' ,3' ,7'
and 9' positions. They are adenine (A) and guanine (G).
m
100. Pyrimidines : They are smaller molecule than purines.
co
These are 6 membered single ringed nitrogenous
bases that contain nitrogen at 1' and 3' positions like
cytosine (C), thymine (T) and uracil (U).
l.
101. ATP was discovered by Karl Lohmann (1929).
ai
102. Formation of ATP is endergonic reaction.
103. Glycogen : It is a branched polymer of glucose and
gm contain 30,000 glucose units. It is also called animal
starch. It is also found as storage product in blue green
algae, slime moulds, fungi and bacteria. It is a non-
reducing sugar and gives red colour with iodine. In
glycogen, glucose molecule are linked by 1 – 4
glycosidic linkage in straight part and 1 – 6 linkage in
the branching part glycogen has branch points about
every 8-10 glucose units.
104. Starch : Starch is formed in photosynthesis and function
as energy storing substance. It is found abundantly in
rice, wheat, legumes, potato (oval and ecentric
shaped), banana, etc. Starch is of two types. Straight
chain polysaccharides known as amylose and branched
chain as amylopectin. Both composed of D – glucose
units jointed by a - 1 - 4 linkage and a - 1 - 6
linkage. It is insoluble in water and gives blue colour
when treated with iodine.
105. Cellulose : An important constituent of cell wall, made
up of unbranched chain of 6000 b–D glucose units
linked by 1 – 4 glycosidic linkage. It is fibrous, rigid and
insoluble in water. It doesn’t give any colour when
treated with iodine. It is a most abundant
polysaccharide.
106. Chitin : It is a polyglycol consisting of N-acetyl–D–
glucosamine units connected with b - 1, 4
glycosidic linkage. Mostly it is found in hard
exoskeleton of insects and crustaceans and some times
in fungal cell wall. Second most abundant
carbohydrate.
19
107. Agar-Agar : It is a galactan, consisting of both D and L
galactose and it is used to prepare bacterial cultures. It
is obtained from cell wall of red algae e.g., Gracilaria,
Gelidium etc.
108. The common sugars in hemicellulose are D-xylose, L–
arabinose, D-galactose, D-mannose and D-glucusonic
acid. e.g., hemicellulose.
109. Gum : It secreted by higher plants after injury or
pathogenic attacks. It is viscous and seals the wound. It
involves sugars like L-arabinose, D-galactose, D-
glucusonic acid. e.g., gum arabic.
124. RNA is second type of nucleic acid which is found in
nucleus as well as in cytoplasm i.e., mitochondria,
plastids, ribosomes etc. They carry the genetic
information in some viruses. They are widely
distributed in the cell. Genomic RNA was discovered by
Franklin and Conrat (1957).
NCERT IMAGES FOR NEET EXAM

m
110. Mucopolysaccharides : These are gelatinous substance,
containing amino sugars, uronic acid, etc. All slimy

co
substances of plant are mucopolysaccharide. e.g.,
hyaluronic acid, vitreous humour, chondridine

l.
sulphate, heparin, husk of isabgol and mucilage also.

ai
111. Protein : Word protein was coined by Berzelius (1838)
and was used by G. J. Mulder first time 1840.
112. 15% - 30% of protoplasm is made up of protein.
Average proteins contain 16% nitrogen, 50–55%
carbon, oxygen 20–24%, hydrogen 7% and sulphur 0.3
gm
4@
– 0.5%.
113. Phosphoprotein : They composed of protein and
phosphate e.g., casein (milk) and vitellin (egg).
8

114. Proteins are the most diverse molecule on the earth.

h2

115. Monelin protein is the sweetest substance obtained

from African berry (2000 time sweeter than sucrose).
us

116. Most abundant protein on earth is RuBisCo

117. Myosin is structural as well as enzymatic protein (ATPase).
118. Nucleic acids were first reported by Friedrich Miescher
ay

(1871) from the nucleus of pus cell. Altmann called it

first time as nucleic acid. Nuclein was renamed nucleic
ia

acid by Altman in (1889). They are found in nucleus.

They help in transfer of genetic information.
in

119. Term DNA was given by Zacharis.

sa

120. Repetitive DNA : This type of arrangement is found near

centromere of chromosome and is inert in RNA
synthesis. The sequence of nitrogenous bases is
repeated several times.
121. Chargaff’s rule : Quantitatively the ratio of adenine (A) to
thymine (T) and guanine (G) to cytosine (C) is equal. i.e.,
“Purines are always equal to pyrimidine”.
122. C value : It is the total amount of DNA in a genome or
haploid set of chromosomes.
123. X-Ray crystallography study of DNA : It was done by
Wilkins. It shows that the two polynucleotide chains of
DNA show helical configuration.

20
 sa
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84@
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21
 sa
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84@
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22