9

Biomolecules
Important Points
1. All the carbon compounds that we get from living tissues can
be called biomolecules.
2. Living tissues also contain inorganic elements and compounds.
How can we conclude this?
(i) One weighs a small amount of a living tissue and dry it.
(ii) All the water evaporates. The remaining material gives dry
weight.
(iii) If tissue is fully burnt. All the carbon compounds are
oxidised to gaseous form CO2 , water vapour and are
removed.
(iv) The remaining ash contains inorganic elements
(like calcium, magnesium, etc).
3. Therefore, elemental analysis gives elemental composition of
living tissues in the form of hydrogen, oxygen, chlorine,
carbon, etc.
4. Amino Acids
(i) Organic compounds containing an amino group and an
acidic group as substituents on the same carbon, i. e. , the
-carbon. Hence, they are called -amino acids.
(ii) They are substituted methanes.
(iii) There are four substituents groups occupying the four
valency positions hydrogen, carboxyl group amino group
and a variable group designated as R group. Based on the
nature of R group, there are many amino acids. However,
20 amino acids occur in protein.

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(iv) R group can be :

(a) Hydrogen (glycine)
(b) Methyl group (alanine)
(c) Hydroxy methyl (serine)
COOH
COOH

H C N H2
H C NH 2

CH3
H
Glycine

Alanine

COOH

H C NH 2

CH3 OH
Serine

(v) Chemical and physical properties:

(a) Based on number of amino and carboxyl groups there
are
Acidic (glutamic acid)
Basic (lysine)
Neutral (valine).
(b) Aromatic amino acid (tyrosine, phenylalanine and
tryptophan).
(c) A particular property-ionizable nature of NH 2 and
COOH groups.
R
R
+

H3 N CH COOH s
H3 N CH COO
(A)
(B)
R

s
H 2N CH COO
(C)
B is called Zwitter ionic form.
5. Lipids Generally, water insoluble; simple fatty acid.
A fatty acid has a carboxyl group attached to an R group.
(i) The R group could be methyl ( CH3 ) or ethyl (C2H5 ) or
higher number of CH 2 group (1 carbon to 19 carbons).
(ii) Fatty acids Saturated (without double bond) and
Unsaturated (with one or more C==C double bonds),
e.g., Trihydroxy propane (glycerol).
(iii) Many lipids have both glycerol and fatty acids.
Here, fatty acids are found esterified with glycerol.
(iv) They can be monoglycerides, diglycerides and triglyceride.
It also called fats high melting point.

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Oils low melting points (e.g., Gingily oil) remain as oil in

winters.
(v) It also called phospholipids Phosphorus and a
phosphorylated organic compound in them.
They are found in cell membranes, e.g., lecithin.
6. Nucleosides Nitrogen base + sugar, e.g., adenosine,
guanosine, thymidine, uridine, cytidine.
7. Nucleotides Nitrogen base + sugar + phosphate group,
e.g., adenylic acid, thymidylic acid, guanylic acid, uridylic acid,
cytidylic acid.
CH2OH
O

OH

HO

HOCH2

OH

OH

OH
C6H12O6 (glucose)

OH

OH

C5H10O5 (ribose)
O
O

CH2OH

CH3(CH2)14COOH
Fatty acid
(palmitic acid)

HOCH2

R2COCH

CHOH

CH2OCR1
Triglycerides (R1, R2
and R3 are fatty acids)

CH2OH
Glycerol

CH2OCR1

Adenine

NH
N
Adenine (purine)
OH
OH
Adenosine

O
HOPOCH2

HOCH2

Uracil

HN
O

Adenine

OH

OH
OH
Adenylic acid

Uracil (pyrimidine)
Nitrogen bases

OH
OH
Uridine
Nucleosides

Nucleotides

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8. Primary Metabolites These are the organic compounds such

as amino acids, sugars, etc.
9. Secondary Metabolites It found in plant, fungal and
microbial cells. These are thousands of compounds other than
primary metabolites, e.g., Alkaloids, flavonoids, rubber,
essential oils, antibiotics, coloured pigments, scents, gums,
spices, etc.
10. Biomacromolecules It found in the acid insoluble fraction
(molecular weights more than one thousand). Include proteins,
nucleic acids, polysaccharides and lipids.
11. Proteins
Polypeptides They are linear chains of amino acids linked by
peptide bonds.
Some Proteins and their Functions
Proteins
Collagen
Trypsin
Insulin
Antibody
Receptors
GLUT-4

Functions
Intercellular ground substance
Enzyme
Hormone
Fights infections against
Sensory reception (smell, taste, hormone, etc.)
Enables glucose transport into cells

12. Polysaccharides
(i) They are long chains of sugars.
(ii) They are threads containing different monosaccharides as
building blocks.
e.g., cellulose = Polymeric polysaccharide consisting of only
one type of monosaccharides, i.e., glucose.
Starch = Presents as a store house of energy in plant
tissues.
Glycogen = Present in animals
Insulin = Polymer of fructose.
(iii) In a polysaccharide chain, right end, reducing end, left end
and non-reducing end.

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CH2OH
O

CH2OH
O

O
O

OH

OH

OH

O
O

OH

OH

CH2

Diagrammatic representation of a portion of glycogen

13. Nucleic Acid

(i) Polynucleotides
(ii) Nucleotide is the building block
(iii) Components of nucleic acid.
(a) Heterocyclic compoundsNitrogenous bases
Purines

Pyrimidines

Adenine
Guanine

Uracil
Cytosine
Thymine

(b) A monosaccharideEither ribose or deoxyribose

Ribose in RNA (ribonucleic acid)
Deoxyribose in DNA (deoxyribonucleic acid)
(c) A phosphoric acid or phosphate
14. Structure of Proteins
(i) Primary structure The sequence of amino acids, i.e.,
the positional information in a protein, which is the first
amino acids, which is second and so on is called the
primary structure.
(a) Protein is imagined as a line left end represented by the
first amino acid also called as N-terminal amino acid.
Right end represented by last amino acid also called as
C-terminal amino acid.

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(b) A protein thread does not exist throughout as an

extended rigid rod.
(c) The thread is folded in the form of a helix.
(d) Some portions are folded as helix.
(ii) Secondary structure Region of proteins other than
helix folds into other forms and are called secondary
structure.
(iii) Tertiary structure Long protein chain is folded upon
itself like a hollow a woolen ball, giving rise to tertiary
structure. This gives us a B-dimensional view of a protein.
This structure is necessary for the many biological
activities of proteins.
(iv) Quaternary structure Some proteins are an assembly of
more than one polypeptide or sub-units. The manner in
which these individual folded polypeptides or sub-units are
arranged with respect to each other is the architecture of
protein otherwise called quaternary structure of a protein.

(a)

(b)

Cartoon showing : (a) A secondary structure and

(b) A tertiary structure of proteins

15. Peptide Bond In proteins or polypeptide, amino acids are

linked by peptide bond which is formed when carboxyl
( COOH) group of one amino acid reacts with amino ( NH 2 )
group of next amino acid with the elimination of a water
moiety (the process is called dehydration).
16. Glycosidic Bond Individual monosaccharides are linked by
glycosidic bond in a polysaccharides.
This bond is also formed by dehydration. This bond is formed
between two carbon atoms of two adjacent monosaccharides.
17. Phosphodiester Bond The bond between the phosphate and
hydroxyl group of sugar is an ester bond. As there is one such
ester bond on either side, it is called phosphodiester.

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18. Structure of DNA

Watson-Crick Model Features
(i) DNA exists as a double helix.
(ii) Two strands of polynucleotides are antiparallel, i.e., run in
the opposite direction.
(iii) Backbone is formed by the sugar-phosphate-sugar chain.
(iv) A and G of one strand base pairs with T and C, respectively
on the other strand.
(v) There are two hyrogen bonds between A and T and three
hydrogen bonds between G and C.
(vi) Each strands appears like a helical staircase.
19. Turnover and Metabolism All biomolecules have a turnover.
This means that they are constantly being changed into some
other biomolecules and also made from some other
biomolecules.
The making and breaking is through chemical reactions
constantly occurring in living organism. Together all these
chemical reactions are called metabolism, e.g., removal of CO2
from amino acid forms amine. Removal of amino group in a
nucleotide base. Hydrolysis of a glycosidic bond in a
disaccharide.
20. Features of Metabolic Reactions Flow of metabolites
through metabolic pathways has a definite rate and direction
like automobile traffic. This metabolite flow is called the
dynamic state of body constituents.
21. Metabolic reactions are catalysed reactions.
(i) Enzymes The catalysts which hastens the rate of a given
metabolic conversion are also proteins. These proteins with
catalytic power are named enzymes.
(ii) Anabolic pathway Formation of complex structure from
a simpler structure, e.g., acetic acid becomes cholesterol.
(iii) Catabolic pathway Degradation of a complex structure
to form a simpler structure, e.g., glucose becomes lactic
acid in our skeletal muscles.
22. ATP (Adenosine Triphosphate) most important form of energy
currency in living systems is the bond energy in ATP.
23. Features of Enzymes
(i) Mostly proteins.
(ii) Nucleic acids that behaves like enzymes are called
riboenzymes.

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(iii) Enzymes have active sites, it is a crevice or pocket into

which the substrate fits.
(iv) Enzymes through active sites catalyse reactions at a high
rate.
(v) Difference between organic and inorganic catalysts
Inorganic catalysts work efficiently at high temperature
and high pressure.
Enzymes gets damaged at high temperature (say above
40C).
24. Chemical Reactions When bonds are broken and new bonds
are formed during transformation, this is called chemical
reactions :
Example Inorganic chemical reaction
Ba(OH)2 + H 2SO4 BaSO4 + 2H 2O
Organic chemical reaction Hydrolysis of starch into
glucose.
Rate of a physical or chemical process = Amount of product
formed per unit time.
P
Rate =
t
25. General Rule of Thumb Rate doubles or decreases by half
for every 10C change in either direction.
26. Catalysed reactions proceed at rates vastly higher than that of
uncatalysed ones.
e.g.,

Carbonic anhydrase

CO2 + H 2O H 2CO3
Carbon
dioxide

Water

Carbonic
acid

In absence of enzyme, reaction slow-200 molecules of H 2CO3

formed in an hour.
In presence of enzyme, reaction fast-600000 molecules formed
every second.
27. Working of Enzymes
(i) Substrate (S) Chemical which is converted into a
product.
(ii) Enzyme Proteins with three dimensional structures
including an active site convert a substrate (S) into a
product (P ).
S P

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(iii) The substrate has to diffuse towards the active site. There
is thus, an obligatory formation of an ES complex. This
complex formation is a transient phenomenon.
(iv) During this state, a new structure of the substrate called
transition state structure is formed.
(v) After bond making/breaking is completed, the product is
released from the active site.
(vi) There could be many more altered structural states
between the stable substrate and the product.
28. Concept of Activation Energy
Transition state

Potential energy

Activation energy without enzyme

Activation energy with enzyme

Substrate (s)

Product (P)
Progress of reaction

Y -axis = Potential energy

X-axis = Progression of the structural transformation or states
through transition state.
Two features to notice
(a) If P is at a lower level than S, the reaction is an exothermic
reaction (no supply of energy is needed to form the product).
(b) Activation energy The difference in average energy content
of S from that of the transition state is called activation
energy.
29. Nature of Enzyme Action
E +
S
s
ES EP E + P
Enzyme Substrate

Enzymesubstrate
complex

Enzymeproduct
complex

Enzyme Product

Steps (catalytic cycle)

(i) Substrate binds to the active sites of the enzyme.
(ii) Binding induces enzyme to alter its shape fitting more
tightly around the substrate.

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(iii) Active site of enzyme breaks the chemical bonds of the

substrate and the new enzyme-product complex is formed.
(iv) Enzyme releases products of the reaction and the free
enzyme is ready to bind to another molecule of the
substrate and run through the catalytic cycle once again.
30. Factors Affecting Enzyme Activity
(i) Temperature and pH.
(a) Each enzyme shows its highest activity a particular
temperature and pH called the optimum temperature
and optimum pH.
(b) Activity declines both below and above the optimum
value.
(b)

Energy activity

(a)

pH

Temperature

Vmax
2

Velocity of reaction (V)

Vmax
(c)

Km

[S]

Effect of change in
(a) pH
(b) temperature
(c) concentration of substrate on enzyme.

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(ii) Concentration of substrate :

(a) With the increase in substrate concentration, the
velocity of the enzymatic reaction. The reaction
ultimately reaches a maximum velocity (V max ) which is
not exceeded by any further rise in concentration of
substrate.
(b) When the binding of the chemical shuts off enzyme
activity, the process is called inhibition and the
chemical is called an inhibitor.
31. Classification and Nomenclature of Enzymes
(i) Oxidoreductases/dehydrogenases Catalyse
oxidoreduction between two substrates S and S , e.g.,
S (reduced) + S (oxidised) S (oxidised) + S (reduced)
(ii) Transferases Catalyse transfer of a group. G (other than
hydrogen) between a pair of substrate S and S , e.g.,
S G + S S + S G
(iii) Hydrolases Catalyse hydrolysis of ester, ether peptide
glycosidic CC, Chalide or PN.
(iv) Lyrases Catalyse removal of groups from substrates
mechanisms other than hydrolysis leaving double bonds.
X Y

C C X Y + C == C
(v) Isomerases Catalyse
inter-conversion
of
optical,
geometric or positional isomers.
(vi) Ligases Catalyse linking together of two compounds,
e.g., enzymes which catalyse joining of CO, CS, CN,
PO, etc, bonds.
32. Co-factors
(i) In some cases, non-protein constituents called co-factors are
bound to the enzyme to make enzyme catalytically active.
(ii) Protein portion is called apoenzyme.
Types of co-factors
(a) Prosthetic group Organic compound,
e.g., peroxidase and catalase and haem is the
prosthetic group.
(b) Co-enzymes Organic
compound,
but
their
association with the apoenzyme is only transient
usually occurring during the course of catalysis.
e.g., Nicotinamide Adenine Dinucleotide (NAD and
NADP).
(c) Metal ions, e.g., zinc is a co-factor for the proteolytic
enzyme carboxypeptidase.

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Exercises
Question 1. What are macromolecules? Give examples.
Answer Chemical compounds, which are found in the acid insoluble
fraction are called macromolecules or biomacromolecules. For example,
proteins, lipids and carbohydrate, etc.

Question 2. Illustrate a glycosidic, peptide and a phosphodiester

bond.
Answer Glycosidic Bond A glycosidic bond is a type of functional
group that joins a carbohydrate (sugar) molecule to another group, which
may or may not be another carbohydrate.
Anomeric
carbon

OH
O

H
HO

H
H

OH

OH

H
+ OH

OH

Glycosidic
bond

OH

CH3
HO

H
OH

OH

+ H 2O
O CH3

Peptide Bond A peptide bond (amide bond) is a chemical bond formed

between two molecules when the carboxyl group of one molecule reacts
with the amine group of the other molecule, thereby releasing a molecule of
water (H 2 O).
O
+

R
OH

H
NR
H

RCNR' + H2O
H

Phosphodiester Bond A phosphodiester bond is a group of strong

covalent bonds between a phosphate group and two other molecules over
two ester bonds. In DNA and RNA, the phosphodiester bond is the linkage
between the 3 carbon atom of one sugar molecule and the 5 carbon of
another, deoxyribose in DNA and ribose in RNA.

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3'

5'

OCH 2

Thymine

.......

Adenine

O
O

O
HO P O

P OH
O
CH 2

5'

Guanine

.......
.......

O
Cytosine

CH 2

3'

CH 2

Diagram indicating secondary structure of DNA

Question 3. What is meant by tertiary structure of proteins?

Answer Tertiary Structure of Proteins Tertiary structure of proteins is
generally stabilised by non-local interactions, most commonly the formation
of a hydrophobic core, but also through salt bridges, hydrogen bonds,
disulphide bonds and even post-translational modifications. The term
tertiary structure is often used as synonymous with the term fold. The
tertiary structure is what controls the basic function of the protein.

A tertiary structure of proteins

Question 4. Find and write down structures of 10 interesting small

molecular weight biomolecules. Find if there is any industry which
manufactures the compounds by isolation. Find out who are the
buyers.

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Answer
CH2OH
O

HO

HOCH2

OH

OH

OH
OH

OH
C5H12O5 (Glucose)
Sugars (carbohydrates)

OH

C5H10O5 (Ribose)

COOH

COOH

HCNH2

COOH

HCNH2

HCNH2

CH2

Glycine

CH2OH

Alanine
Amino acids

Serine

O
CH3(CH2)14COOH

CH2OH

Fatty acid
(Palmitic acid)

CHOH

CH2OCR1

R2COCH

CH2OCR3

CH2OH
Glycerol

Triglyceride (R1, R2
and R3 are fatty acids)

O
O

CH2OCR1

R2COCH

CH2OPOCH2CH2
OH
Phospholipid (lecithin)

N
CH3

Cholesterol

CH3 HO

CH3

Fats and oils (lipids)

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NH2
N

HOCH2

Adenine

NH

Adenine (purine)

OH

OH

Adenosine

O
HOCH3

Uracil

Adenine

OH

HN
O

HOPOCH2

N
OH

Uracil (pyrimidine)
Nitrogen bases

OH

Uridine
Nucleosides

OH

OH

Adenylic acid
Nucleotide

Diagrammatic representation of small molecular weight

There are many industries who make these biomolecules

now-a-days these biomolecules are used in many drugs, injections,
medicines, food preparation so are used by several people.

Question 5. Proteins have primary structure. If you are given a

method to know which amino acid is at either of the two termini
(ends) of a protein, can you connect this information to purity or
homogeneity of a protein?
Answer The sequence of amino acids, i.e., the positional information in a
protein which is the first amino acid, which is second and so on is called the
primary structure of a protein. The first amino acid is also called as
N-terminal amino acid. The last amino acid is called the C-terminal amino
acid. Yes, we can connect this information to purity or homogeneity of a
protein. Based on number of amino and carboxyl groups, there are acidic
(e.g., glutamic acid), basic (lysine) and neutral (valine) amino acids,
proteins may be acidic, basic and neutral.

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Question 6. Find out and make a list of proteins used as therapeutic

agents. Find other applications of proteins (e.g., cosmetics, etc.)
Answer

Some Proteins and their Functions

Protein

Functions

Collagen
Trypsin
Insulin
Antibody
Receptor
GLUT-4

Intercellular ground substance

Enzyme
Hormone
Fights infectious agents
Sensory reception (smell, taste, hormone, etc.)
Enables glucose transport into cells

Question 7. Explain the composition of triglyceride.

Answer Triglycerides are composed of two types of molecules,
i.e., glycerol (3 carbon molecules) and fatty acids which attach to the
glycerol at the alcohol unit. The following is a structural representation of a
triglyceride at the molecular level
1

H3CCHCH2
O O
O

O
O C

Fatty acids are chains of hydrocarbons 4-22 (or more) carbons a long with a
carboxyl group at one end. If each carbon has two hydrogen atoms, the
fatty acid is saturated. If two carbon atoms are double-bonded, so that
there is less hydrogen in the fatty acid, it is unsaturated (monounsaturated).
If more than two carbon atoms are unsaturated, the fatty acid is
polyunsaturated.

Question 8. Can you describe what happens when milk is converted

into curd or yoghurt, from your understanding of proteins.
Answer Milk contains a protein called casein. This protein gives milk its
characteristic white colour. It is of high nutritional value because it contains

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all the essential amino acids required by mans body. The curd forms
because of the chemical reaction between lactic acid bacteria and casein.
When curd is added to milk, the lactic acid bacteria present in it cause
coagulation of casein and thus, convert it into curd.

Question 9. Can you attempt building models of biomolecules using

commercially available atomic models (Ball and stick models).

Answer Yes, we can make models of biomolecules using commercially
available atomic models.

Question 10. Attempt titrating an amino acid against a weak base

and discover the number of dissociating (ionisable) functional groups

in the amino acid.
Answer When an amino acid is titrated against a weak base, it
dissociates and gives two functional groups:
(i) COOH group (carboxylic group)
(ii) Amino group (NH2 ).

Question 11. Draw the structure of the amino acid and alanine.
Answer
R-group
or side chain
-carbon

-hydrogen

H3NCHCO
-amino
group

Carboxyl
group

Question 12. What are gums made of? Is fevicol different?

Answer Gums are made of carbohydrates, i.e., L-rhamnose, D-galactose
and D-galacturonic acid, etc. Fevicol is different from natural gums. It is a
synthetic product.

Question 13. Find out a qualitative test for proteins, fats and oils

and starch amino acids and test any fruit juice, saliva, sweat and
urine for them.
Answer

A qualitative test for proteins.

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(i) Xanthoproteic Test

Experimental Material
(a) Urine
(b) Water

Observation
Inference
Yellow precipitate Formation of yellow precipitate
indicates the presence of protein in
No precipitate
the food material.

(ii) A qualitative test for fats.

Emulsification Test
Experimental Material
(a) Sweat
(b) Water

Observation
Oil droplets
No oil droplet

Inference
Formation of oil droplets,
i.e., emulsification indicates the
presence of fats in the given food
material.

(iii) A qualitative test for oils.

Paper Test
Experimental Material
Observation
(a) Food material (sample) Paper becomes
translucent
(b) Water

Inference
Opaque paper becomes
translucent which indicates the
presence of fats in the food
material.

(iv) A qualitative test for starch.

Iodine Test
Experimental Material
(a) Fruit juices
(b) Water

Observation
Blue black
colour

Inference
Formation of blue black colour
indicates the presence of starch in
the given food material.

Question 14. Find out how much cellulose is made by all the plants

in the biosphere and compare it with how much of paper is

manufactured by man and hence, what is the consumption of plant
material by man annually. What a loss of vegetation?
Answer Most paper is formed from wood pulp. The main component of
wood pulp is cellulose, a polymer made of many glucose molecules linked
together. The cellulose molecules and their bonding to each other give
paper its properties.
About 33% of all plant matter is cellulose.
The cellulose content of cotton is 90% and that of wood is 40-50%. For
industrial use, cellulose is mainly obtained from wood pulp and cotton. It is
mainly used to produce paperboard and paper; to a smaller extent. It is
converted into a wide variety of derivative products such as cellophane and
rayon.

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Question 15. Describe the important properties of enzymes.

Answer
(i) Enzymes are proteins which catalyse biochemical reactions in the
cells.
(ii) They are denatured at high temperatures.
(iii) Enzymes generally function in a narrow range of temperature and pH.
Each enzyme shows its highest activity at a particular temperature
and pH called the optimum temperature and optimum pH.
(iv) With the increase in substrate concentration, the velocity of the
enzymatic reaction rises at first. The reaction ultimately reaches a
maximum velocity (v max ) which is not exceeded by any further rise in
concentration of the substrate.
(v) The activity of an enzyme is also sensitive to the presence of specific
chemicals that bind to the enzyme.
(vi) Enzymes are substrate specific in their action.

Selected NCERT Exemplar Problems

Very Short Answer Type Questions
Question 1. Medicines are either man made (i.e., synthetic) or
obtained from living organisms like plants, bacteria, animals, etc.,
and hence, the latter are called natural products. Sometimes, natural
products are chemically altered by man to reduce toxicity or side
effects. Write against each of the following whether they were
initially obtained as a natural product or as a synthetic chemical.
(i) Penicillin ........... synthetic chemical.
(ii) Sulphonamide ............ synthetic chemical.
(iii) Vitamin-C ............. natural product ..............
(iv) Growth hormone ............. natural product ..........
Answer (i) Penicillin
(ii) Sulphonamide
(iii) Vitamin-C
(iv) Growth hormone

Natural product
Synthetic chemical
Natural product
Natural product

Question 2. Select an appropriate chemical bond among ester bond,

glycosidic bond, peptide bond and hydrogen bond and write against
each of the following.

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(i) Polysaccharide ............... (ii) Protein ...................

(iii) Fat ...................
(iv) Water ...................
Answer

(i) Polysaccharide
(ii) Protein

Glycosidic bond

Peptide bond

(iiii) Fat

Ester bond

(iv) Water

Hydrogen bond.

Question 3. Write the name of any one amino acid, sugar,

nucleotide and fatty acid.
Answer Alanine is an amino acid, purine is a nucleotide and linolenic acid
is a fatty acid.

Question 4. Reaction given below is catalysed by oxidoreductase

between two substrates A and A , complete the reaction.
A reduced + A oxidised
Answer

A reduced + A oxidised A oxidised + A reduced

Question 5. How are prosthetic groups different from co-factors?

Answer

Differences between prosthetic groups and co-factors

Prosthetic Groups Prosthetic groups are organic compounds and are

distinguished from other co-factors in that they are tightly bound to the
apoenzyme.
Co-factors Enzymes are composed of one or several polypeptide chains.
However, there are a number of cases in which non-protein constituents
called co-factors are bound to the enzyme to make the enzyme catalytically
active.

Question 6. Glycine and alanine are different with respect to one

substituent on the -carbon. What are the other common substituent
groups?
Answer There are four substituent groups occupying the four valency
positions in an amino acid. These are hydrogen, carboxyl group, amino
group and a variable group designated as R group. The R group in amino
acid glycine is a hydrogen and a methyl group in case of amino acid
alanine, etc.

Question 7. Starch, cellulose, glycogen, chitin are polysaccharides

found among the following. Choose the one appropriate and write
against each.

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Cotton fibre ...................

Exoskeleton of cockroach ...................
Liver ...................
Peeled potato ...................
Answer

Cotton fibre
Exoskeleton of cockroach
Liver
Peeled potato

Cellulose
Chitin
Glycogen
Starch

Short Answer Type Questions

Enzyme activity

Question 1. Enzymes are proteins. Proteins are long chains of amino

acids linked to each other by peptide bonds. Amino acids have many
functional groups in their structure. These functional groups are
many of them at least, ionisable. As they are weak acids and bases in
chemical nature, this ionisation is influenced by pH of the solution.
For many enzymes, activity is influenced by surrounding pH. This is
depicted in the curve below, explain briefly.

pH

Answer Enzymes, generally function in a narrow range of pH. Each

enzyme shows its highest activity at a particular the optimum pH. Activity
declines both below and above the optimum value. The graph shows
maximum enzyme activity at optimum pH. The rate of enzyme activity
decreases above and below that of optimum pH.

Question 2. Is rubber a primary metabolite or a secondary

metabolite? Write four sentences about rubber.
Answer
(i) Yes, It natural rubber (cis-1, 4-polyisoprene) is a secondary
metabolite. It is extracted from the rubber tree (Hevea brasiliensis).
(ii) In the rubber tree, latex is produced in the highly specialised cells,
called laticifers in phloem.

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(iii) Rubber is a terpenoid and due to its high tensile strength, elasticity
and plasticity properties it is widely used in industries.
(iv) It is a polymeric substance.

Question 3. Schematically represent primary, secondary and

tertiary structures of a hypothetical polymer say for example a
protein.
Answer

Structure of Proteins

Primary Structure The sequence of amino acids, i.e., the positional

information in a protein, which is the first amino acid, which is second and
so on is called the primary structure of a protein. The first amino acid is also
called as N-terminal amino acid. The last amino acid is called the
C-terminal amino acid.
Secondary Structure Regularly repeating local structures stabilised by
hydrogen bonds. The most common examples are the alpha helix, beta
sheet and turns. Because secondary structures are local, many regions of
different secondary structure can be present in the same protein molecule.
Tertiary Structure Tertiary structure is generally stabilised by non-local
interactions, most commonly the formation of a hydrophobic core, but also
through salt bridges, hydrogen bonds, disulphide bonds and even
post-translational modifications. The term tertiary structure is often used as
synonymous with the term fold. The tertiary structure is what controls the
basic function of the protein.

N
C

Primary structure

Secondary structure

Tertiary structure

Question 4. Nucleic acids exhibit secondary structure, justify with

example.
Answer For nucleic acids, the building block is a nucleotide. A nucleotide
has three chemically distinct components. One is a heterocyclic
compound, the second is a monosaccharide and the third a phosphoric
acid or phosphate.
The heterocyclic compounds in nucleic acids are the nitrogenous bases
named adenine, guanine, uracil, cytosine and thymine. Adenine and
guanine are substituted purines while the rest are substituted pyrimidines.

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The skeletal heterocyclic ring is called as purine and pyrimidine

respectively. The sugar found in polynucleotides is either ribose
(a monosaccharide pentose) or 2' deoxyribose. A nucleic acid containing
deoxyribose is called deoxyribonucleic acid (DNA) while that which
contains ribose is called ribonucleic acid (RNA).

Question 5. Comment on the statement living state is a

non-equilibrium steady state to be able to perform work.
Answer The most important fact of biological systems is that all living
organisms exist in a steady-state characterised by the concentrations of
each of these biomolecules. These biomolecules are in a metabolic flux.
Any chemical or physical process moves spontaneously to equilibrium. The
steady state is a non-equilibrium state.
As living organisms work continuously, they cannot afford to reach
equilibrium. Hence, the living state is a non-equilibrium steady-state to be
able to perform work. This is achieved by energy input. Metabolism
provides a mechanism for the production of energy. Hence, the living state
and metabolism are synonymous. Without metabolism, there cannot be a
living state.

Long Answer Type Questions

Question 1. Formation of Enzyme-Substrate complex (ES) is the
first step in catalysed reactions. Describe the other steps till the
formation of product.
Answer
Mechanisms of Enzymatic Action The catalytic cycle of an enzyme action
can be described in the following steps
(i) First, the substrate binds to the active site of the enzyme, fitting into
the active site.
(ii) The binding of the substrate induces the enzyme to alter its shape,
fitting more tightly around the substrate.
The formation of the ES complex is essential for catalysis.
E+S

ES EP E + P

(iii) The active site of the enzyme, now in close proximity of the substrate
breaks the chemical bonds of the substrate and the new enzyme
product complex is formed.
(iv) The enzyme releases the products of the reaction and the free
enzyme is ready to bind to another molecule of the substrate and run
through the catalytic cycle once again.

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Question 2. What are different classes of enzymes? Explain any two

with the type of reaction they catalyse.
Answer

Classification and nomenclature of enzymes

Enzymes are divided into six classes each with 4-13 sub-classes and
named accordingly by a four-digit number.
Oxidoreductases/dehydrogenases Enzymes
which
oxidoreduction between two substrates S and S' , e.g.,

catalyse

S reduced + S oxidised S oxidised + S' reduced

Transferases Enzymes catalysing a transfer of a group, G (other than

hydrogen) between a pair of substrate S and S' , e.g.,
S-G + S' S + S' - G

Hydrolases Enzymes catalysing hydrolysis of ester, ether, peptide,

glycosidic, CC, Chalide or PN bonds.
Lyases Enzymes that catalyse removal of groups from substrates by
mechanisms other than hydrolysis leaving double bonds.
Isomerases Includes all enzymes catalysing interconversion of optical,
geometric or positional isomers.
Ligases Enzymes catalysing the linking together of two compounds,
e.g., enzymes which catalyse joining of CO, CS, CN, PO, etc.,
bonds.

Question 3. Nucleic acids exhibit secondary structure. Describe

through Watson-Crick model.
Answer

Watson and Crick model of DNA Structure

James Watson and Francis Crick proposed a structure for the DNA
molecule that suggested the basic mechanism of DNA replication.
According to them
(i) DNA is composed of two strands of DNA running anti-parallel
(remember the 5' and 3' -ends) to each other.
(ii) The hydrophilic sugar (ribose) and phosphate groups of the
nucleotides are face the outside of the molecule and the relatively
hydrophobic nitrogenous bases are on the inside of the molecule,
hidden from water.
(iii) The nucleotides within each strand are held together by the
phosphodiester bonds between the 5 carbon of one nucleotide and
the 3 carbon of the adjacent nucleotide.
(iv) These strong covalent bonds form the glue that holds the
sugar/phosphate backbone together and thus act to keep each
strand together.

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(v) The two strands of DNA are held
together by weak hydrogen bonds
between the nitrogenous bases.
(vi) These hydrogen bonds are base
specific. That is A (adenine) can
only form hydrogen bonds with T
(thymine) and C (cytosine) can
only form bonds with G (guanine).
(vii) The strands in such a molecule are
said to be complementary.
(viii) The two strands wrap around each
other to form a double helix
structure.
(ix) Watson and Crick explained
Chargraff's Rule of DNA in which
the amount of A in any DNA
sample always equal to the
amount of T and that the amount of
G always equal to the amount of C.

Sugar-phosphate
backbone
(two; outside)

Nitrogenous
base-pairs
(inside)

A+T
G+C

Held together by
hydrogen bonds
(H-bonds)
Structure of DNA

Question 4. What is the differences

between a nucleotide and nucleoside? Give two examples of each with

their structure.
Answer

Nucleotides are building blocks of nucleic acids (DNA and RNA).

Differences between Nucleotide and Nucleoside

Nucleotide

Nucleoside

A nucleotide consists of a nitrogenous

base, a sugar (ribose or deoxyribose)
and one to three phosphate groups
(i.e., sugar + base + phosphate).
Examples adenine, guanine,
cytosine, uracil and thymine.

A nucleoside consists of a nitrogenous base

covalently attached to a sugar (ribose or
deoxyribose) but without the phosphate group
(i.e., sugar + base).
Examples cytidine, uridine, adenosine,
guanosine, thymidine and inosine.

O
HOPOCH2

Adenine

HOCH2

Adenine

OH

OH
OH
Adenylic acid

OH
OH
Adenosine