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Biomolecules: Definitions

1) Carbohydrates are essential biomolecules that serve as an energy source. They include sugars, starch, and cellulose. 2) Carbohydrates can be classified as monosaccharides, oligosaccharides, or polysaccharides depending on their structure. Monosaccharides like glucose cannot be broken down further. 3) Glucose is a particularly important monosaccharide that is used as an energy source in cellular metabolism and is found abundantly in nature. It can be produced commercially from the hydrolysis of starch or sucrose.

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0% found this document useful (0 votes)
416 views50 pages

Biomolecules: Definitions

1) Carbohydrates are essential biomolecules that serve as an energy source. They include sugars, starch, and cellulose. 2) Carbohydrates can be classified as monosaccharides, oligosaccharides, or polysaccharides depending on their structure. Monosaccharides like glucose cannot be broken down further. 3) Glucose is a particularly important monosaccharide that is used as an energy source in cellular metabolism and is found abundantly in nature. It can be produced commercially from the hydrolysis of starch or sucrose.

Uploaded by

Saket Dubey
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd
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Biomolecules

INTRODUCTION
y Living systems are made up of various Definitions
complex biomolecules like carbohydrates,
proteins, nucleic acids, lipids, etc. Chemically, the carbohydrates
y Proteins and carbohydrates are essential may be defined as optically
constituents of our food. active polyhydroxy aldehydes
y In addition, some simple molecules like or ketones or the compounds
vitamins and mineral salts also play an which produce such units on
important role in the functions of organisms. hydrolysis.

CARBOHYDRATES
y Carbohydrates (hydrates of carbon) are
naturally occurring compounds having
general formula Cx(H2O)y, which are constantly
produced in nature & participate in many
important bio-chemical reactions.
Ex. Glucose C6H12O6 C6(H2O)6
Fructose C6H12O6 C6(H2O)6 Concept Ladder
Cellulose and Starch (C6H10O5)n
y Sucrose (Cane sugar) – C12H22O11, and Maltose Saccharin is not
(Malt Sugar) C12(H2O)11 carbohydrate but is
y But some compounds which have formula 500 times sweeter than
according to Cx(H2O)y are not known as sucrose.
carbohydrate
Ex. CH2O Formaldehyde
C2(H2O)2 Acetic acid
C3(H2O)3 Lactic acid
y There are many compounds, which shows
chemical behaviour of carbohydrate but do
not confirm the general formula Cx(H2O)y such
as –
C5H10O4 (2-deoxyribose)
C6H12O5 (Rahmnose) Previous Year’s Questions
y Carbohydrates, the energy source of living
beings, are the most abundant organic Whcih of the following is the
compound around us. sweetest sugar?
y In metabolic process in the living beings, [AIPMT]
glucose is usually oxidized into carbon dioxide (1) Fructose (2) Glucose
and water to provide energy to the cell for (3) Sucrose (4) Maltose
Biomolecules

their functioning.

1.
Classification of Carbohydrates
Carbohydrates are classified on the basis of
their behaviour on hydrolysis.

Monosaccharides (simple sugars)


y These are the sugars which cannot be
hydrolysed into smaller molecules. General
formula is CnH2nOn.
y About 20 monosaccharides are known to
occur in nature. Some common examples are Concept Ladder
glucose, fructose, ribose, etc.
y If −CHO group is present in monosaccharide, Glucose — grape sugar or
dextrose.
then it is known as aldose. Fructose — fruit sugar.
− C− Lactose — milk sugar.
y If || group is present in monosaccharide,
O

then it is known as ketose.

Carbon atoms General term Aldehyde Ketone

3 Triose Aldotriose Ketotriose


4 Tetrose Aldotetrose Ketotetrose
5 Pentose Aldopentose Ketopentose
Biomolecules

6 Hexose Aldohexose Ketohexose


7 Heptose Aldoheptose Ketoheptose

2.
Oligosaccharides
y These are the sugars which yields 2-10 Concept Ladder
monosaccharides units on hydrolysis.
y The two monosaccharide units obtained on
A group of polysaccharides
hydrolysis of a disaccharide may be same or
which are not so widely
different.
used in nature is pentosans
For example,
Hydrolysis
(C5H8O4)n Monosaccharides.
Sucrose → Glucose + Fructose

(a) Disaccharides : Two monosaccharide unit on


hydrolysis (may or may not be same).
Ex. Sucrose, Maltose
(b)Trisaccharides : Three monosaccharide unit
on hydrolysis.

Polysaccharides
y These are the non-sugars which yield a large
no of monosaccharide units on hydrolysis.
y Carbohydrates which yield a large number
Rack your Brain
of monosaccharide units on hydrolysis are
called polysaccharides.
y Polysaccharides are not sweet in taste, hence What is invert sugar and why is it
they are also called non-sugars. so named?
y General formula – (C6H10O5)n.
Ex. Starch, Cellulose, Glycogen etc.

Reducing and Non-Reducing Sugars


y Those sugars or carbohydrates which reduce
Fehling’s solution and Tollens reagent are
referred to as reducing sugars.
y All monosaccharides whether aldose or
ketose are reducing sugars.
y In disaccharides, if the reducing groups of
monosaccharides i.e., aldehydic or ketonic Previous Year’s Questions
groups are bonded, these are nonreducing
sugars. e.g., sucrose. Which one given below is a non-
reducing sugar?
GLUCOSE [NEET(I)-2016]
y Glucose occurs freely in nature as well as in (1) Glucose (2) Sucrose
Biomolecules

the combined form. (3) Maltose (4) Lactose


y It is present in sweet fruits and honey.

3.
y Ripe grapes also contain glucose in large
amounts so it is known as grapes sugar. Rack your Brain
y Glucose is the unit of starch, cellulose and
glycogens. Fructose contain a keto group
but still it reduces Tollens’
Preparation of Glucose reagent. Why?
(1) From Sucrose (Cane sugar)
y If sucrose is boiled with dilute HCl or H2SO4 in
alcoholic solution, glucose and fructose are
obtained in equal amounts.
+
H
C12H22O11 + H2O → C6H12O6 + C6H12O6
Sucrose Glucose Fructose

(2) From Starch


y Commercially glucose is obtained by Concept Ladder
hydrolysis of starch by boiling it with dilute
H2SO4 at 393 K under pressure.
The carbonyl group of
(C6H10O5 )n
+
H
+ nH2O 
393 K; 2−3 atm
→ nC6H12O6 aldoses and ketoses can
Glucose be reduced by the usual
Starch or cellulose
carbonyl-group reducing
Structure of Glucose agents (eg., NaBH4). The
y Glucose is an aldohexose and is also known product of the reduction is
as dextrose. a polyalcohol, known as an
y It is the monomer of many of the larger alditiol.
carbohydrates, namely starch, cellulose.
y It is probably the most abundant organic
compound on earth.
y Its molecular formula was found to be C6H12O6.

Previous Year’s Questions

Reactions of Glucose
Sucrose on hydrolysis gives
(1) Oxidation
[NEET-2020]
y On oxidation with nitric acid, glucose as well
(1) b-D-glucose + a-D-fructose
as gluconic acid both yield a dicarboxylic acid,
(2) a-D-glucose + b-D-glucose
Biomolecules

saccharic acid.
(3) a-D-glucose + b-D-fructose
y This indicates the presence of a primary
(4) a-D-fructose + b-D-fructose
alcoholic (–OH) group in glucose.

4.
Previous Year’s Questions

Fructose reduces Tollens’ reagent


due to
[AIPMT-2010]
(1) Asymmetric carbons
(2) Primary alcoholic group
(3) Secondary alcoholic group
(4) Enolisation of fructose
followed by conversion to
aldehyde by base.

Rack your Brain

A monosaccharide has a
molecular weight of 150. Also
itwas not optically active.
What is the structure of
monosaccharide?

y The exact spatial arrangement of different —


OH groups was given by Fischer after studying
many other properties. Its configuration is
correctly represented as I. So gluconic acid
is represented as II and saccharic acid as III.
Concept Ladder

The change in specific


rotation of an opticaly
active compound in
solution with time to an
equilibrium alue is called
Biomolecules

mutarotation.

5.
(2) Reduction
y On prolonged heating with HI, it forms
Concept Ladder
n-hexane. (Straight Chain)

Glucose in aqueous solutin


is reduced with sodium
amalgam to hexahydric
alcohol sorbitol.

Rack your Brain

What is the product formed on


(3) Cyanohydrin Formation
y Adds a molecule of hydrogen cyanide to give oxidation of glucose with mild
cyanohydrin. oxidizing agent such as Br2
water?

(4) Oxime Formation Previous Year’s Questions


y Glucose reacts with hydroxylamine to form
an oxime.
Glucose molecule reacts with X
number of molecules of phenyl
hydrazine to yield osazone. the
value of X is
[AIPMT]
Biomolecules

(1) two (2) one


(3) four (4) three

6.
(5) Reaction with phenylhydrazine (formation of
osazone) Rack your Brain

What is the product formed
when glucose react with excess
amount of phenyl hydrazine?

(6) Acetylation
y Acetylation of glucose with acetic anhydride
gives glucose pentaacetate which confirms
the presence of five –OH groups.
y Five –OH groups should be attached to Concept Ladder
different carbon atoms.
Glucose pentaacetate
cannot be converted
into the open chain form
because its anomeric
hydroxyl group (i.e. C1–OH)
is acetylated and hence
Stereochemistry of Carbohydrates does not form the oxime.
D & L Sugars
Aldotriose (Smallest carbohydrate)
Ex.

Fischer projection
Definition

The series of aldoses or ketoses


in which the configuration of the
penultimate C-atom (C-next to
CH2-OH group) is described as
D-sugars if -OH is towards RHS
Biomolecules

& L-sugars if it is towards LHS.

7.
Aldotetros
Types of Aldotetrose
(i) Erythrose
(ii) Threoese

No. of C* = 3 (in Aldopentose)


No. of optical isomers 23 = 8
No. of D Sugars = 4
no. of L-Sugars = 4
D-Aldopentose
Biomolecules

All Isomeric D-Sugars are diastereomers.

8.
Aldohexose

No. of C* = 4
No. of stereoisomers = 24 = 16
No. of D-sugars = 8
No. of L-sugars = 8
Cyclic Structure of Glucose Concept Ladder
The structure of glucose explained most of
its properties but the following reactions and
The two cyclic hemiacetal
facts could not be explained by this structure.
forms of glucose differ
y The pentaacetate of glucose does not react
only in the configuration of
with hydroxylamine indicating the absence of
the hydroxyl group at C1,
free —CHO group.
called anomeric carbon.
y Glucose is found to exist in two different
Such isomers, i.e., a-form
crystalline forms which are named as a and b.
and b-form, are called
anomers.
a-D(+) Glucose
The a-form of glucose (m.p. 419 K) is obtained
by crystallisation from concentrated solution
of glucose at 303 K. Previous Year’s Questions

b-D(+) Glucose a-D-glucose and b-D-glucose


The b-form (m.p. 423 K) is obtained by are
crystallisation from hot and saturated [AIPMT]
aqueous solution at 371 K. (1) Epimers (2) Anomers
(3) Enantiomers (4) Diastereomers
Biomolecules

9.
Howarth Structure
y The six membered cyclic structure of glucose Previous Year’s Questions
is called pyranose structure (α– or β–), , in
analogy with pyran. Which one of the following does
y Pyran is a cyclic organic compound with one not exhibit the phenomenon of
oxygen atom and five carbon atoms in the mutarotation?
ring. [AIPMT]
y The cyclic structure of glucose is more (1) (+)-Sucrose (2) (+)-Lactose
correctly represented by Haworth structure (3) (+)-Maltose (4) (-)-Fructose
as given below.

FRUCTOSE
y Fructose is an important ketohexose. It also
has the molecular formula C6H12O6.
y It is obtained by the hydrolysis of disaccharide.
Hydrolysis
Ex : Sucrose → Glucose + Fructose Concept Ladder

y It is a natural monosaccharide found in fruits,


honey and vegetables. All the monosaccharides,
whether aldoses
Structure of Fructose and ketoses, in their
y On the basis of its reactions it was found to hemiacetal and hemiketal
forms behave as reducing
Biomolecules

contain a ketonic functional group at carbon


number 2 and six carbons in straight chain carbohydrates.

10.
as in the case of glucose. It belongs to
D-series and is a laevorotatory compound. It Concept Ladder
is appropriately written as D-(–)-fructose.

D-fructose exists in two


stereoisomeric forms, i.e.,
a-D-fructopyranose and
b-D-fructopyranose.

Cyclic Structure of Fructose


y It also exists in two cyclic forms which are
obtained by the addition of —OH at C5 to the
ketonic group.

Howarth Structure
y The ring formed is a five membered ring and
is named as furanose with analogy to the
compound furan. Furan is a five membered
cyclic compound with one oxygen and four
carbon atoms.

Biomolecules

11.
Comparison of Glucose and Fructose

S.NO. Property Glucose Fructose

1 Molecular formula C6H12O6 C6H12O6

2 Nature Polyhydroxy aldehyde Polyhydroxy ketone

3 Melting point 146°C 102°C

4 Optical nature Dextro rotatory Levo rotatory

5 Molisch test Violet colour Violet colour

6 Tollen’s reagent Silver mirror Silver mirro

7 Fehling’s solution Red ppt Red ppt

8 Phenyl hydrazine Forms osazone Forms osazone

Mixture of glycolic
Oxidation by acid, Tartaric acid and
9 Saccharic acid
conc. HNO3 Trihydroxy Gluteric
acid

DISACCHARIDES
y The two monosaccharides are joined together
by an oxide linkage formed by the loss of a
water molecule.
y These two monosaccharides are held together Rack your Brain
by glycosidic linkage (oxide linkage) through
Biomolecules

oxygen atom. Are all disaccharides sugars?

12.
y In disaccharides, if the reducing groups of
monosaccharides i.e., aldehydic or ketonic Concept Ladder
groups are bonded. These are non-reducing
sugars, e.g., sucrose.
y On the other hand, sugars in which these Sucrose is an naturally
functional groups are free, are called reducing occurring sugar found
sugars, for example, maltose and lactose. in various amounts in
plants like fruits and also
(1) Sucrose produced commercially
y Sucrose which on hydrolysis gives equimolar from sugar cane and sugar
mixture of D(+) glucose and D(-) fructose. beets.
+
H
C12H22O11 + H2O → C6H12O6 + C6H12O6
Sucrose D(+)-Glucose D(–)-Fructose

y These two monosaccharides are held together


by a glycosidic linkage between C1 of α-D-
glucose and C2 of β-D-fructose.
y Since the reducing groups of glucose and
fructose are involved in glycosidic bond
formation, sucrose is a non reducing sugar.

Previous Year’s Questions

Which one of the following


sets of monosaccharides forms
sucrose?
y Sucrose is dextrorotatory but after hydrolysis [AIPMT-2012]
gives dextrorotatory glucose and laevorotatory (1) a
 -D-galactopyranose and
fructose. a-D-glucopyranose
y Since the laevorotation of fructose (–92.4°) is (2) a
 -D-glucopyranose and b-D-
more than dextrorotation of glucose (+ 52.5°), fructofuranose
the mixture is laevorotatory. (3) b
 -D-glucopyranose and a-D-
y Thus, hydrolysis of sucrose brings about a fructofuranose
(4) a
 -D-glucopyranose and b-D-
Biomolecules

change in the sign of rotation, from dextro


(+) to laevo (–) and the product is named as fructofuranose
invert sugar.

13.
(2) Maltose
y Maltose is composed of two α-D-glucose Concept Ladder
units in which C1 of one glucose (I) is linked
to C4 of another glucose unit (II).
Maltose can be broken
y The free aldehyde group can be produced at
down to glucose by the
C1 of second glucose in solution and it shows
maltase enzyme, which
reducing properties so it is a reducing sugar.
catalyses the hydrolysis of
the glycosidic bond.

Rack your Brain



Is maltose sweeter than glucose?
(3) Lactose
y Lactose is found in milk so it commonly
known as milk sugar.
y It is composed of β-D-galactose and β-D-
glucose.
y The linkage is between C1 of galactose and
C4 of glucose. Free aldehyde group may be
produced at C1 of glucose unit, hence it is
also a reducing sugar. Concept Ladder

Unabsorbed lactose
passing through the
intestinal tract with little
lactase causes colic
(severe pain in the stomach
and bowels) diarrhoea and
other interstinal problems.
This is called lactose
intolerance. This happens
in older people.
Biomolecules

14.
POLYSACCHARIDES
y Polysaccharides contain a large number of Concept Ladder
monosaccharide units joined together by
glycosidic linkages. They mainly act as the
Starch is a non-reducing
food storage or structural materials.
saccharide. it neither
reduces Tollens’ reagent
(1) Starch
(or Fehling’s solution) nor
y Starch is the main storage polysaccharide of
forms an osazone.
plants.
y It is the most important dietary source for
human beings. High content of starch is found
in cereals, roots, tubers and some vegetables.
y It is a polymer of α-glucose and consists of
two components—Amylose and Amylopectin.

Amylose
y Amylose is water soluble component which Rack your Brain
constitutes about 15-20% of starch.
y Chemically amylose is a long unbranched What is the inclusion complex?
chain with 200-1000 α-D-(+)-glucose units
held together by C1–C4 glycosidic linkage.

Amylopectin
y Amylopectin is insoluble in water and
constitutes about 80- 85% of starch.
y It is a branched chain polymer of α-D-glucose
units in which chain is formed by C1–C4
glycosidic linkage whereas branching occurs
Biomolecules

by C1–C6 glycosidic linkage.

15.
(2) Cellulose
y Cellulose occurs exclusively in plants and it is
the most abundant organic substance in plant
kingdom. It is a predominant constituent of Previous Year’s Questions
cell wall of plant cells.
y Cellulose is a straight chain polysaccharide Cellulose is polymer of
composed only of β-D-glucose units which [AIPMT]
are joined by glycosidic linkage between C1 of (1) Glucose (2) Fructose
one glucose unit and C4 of the next glucose (3) Ribose (4) Sucrose
unit.

Q1 What are disaccharides? Give one example.

Sol. Disaccharides on hydrolysis give two molecules of the same


monosaccharides. For example, sucrose, maltose, lactose, etc.
or different

Q2 Which of the two components of starch is water soluble?

Sol. Amylose is water soluble but amylopectin is water insoluble.


Biomolecules

16.
Concept Ladder

Excess glucose gets stored


in the liver as glycogen or,
with the help of insulin,
converted into fatty acids,
circulated to other parts of
the body and stored as fat
in adipose tissue.

(3) Glycogen Rack your Brain


y The carbohydrates are stored in animal body
as glycogen. Why is glucose stored as
y It is also known as animal starch because glycogen ?
its structure is similar to amylopectin and is
rather more highly branched.
y It is present in liver, muscles and brain. When
the body needs glucose, enzymes break the
glycogen down to glucose.
y Glycogen is also found in yeast and fungi.

Q3 What is Molisch test? Explain.

Sol. All carbohydrates, i.e., monosaccharides, oligosaccharides and polysaccharides


are characterised by Molisch test. A 1% alcoholic solution of a-naphthol is
called Molisch reagent. When Molisch reagent is added to an aqueous solution
or suspension in water of a carbohydrate followed by conc. H2SO4 along the
Biomolecules

sides of the test tube, a violet ring is formed at the junction of the two layers.

17.
Reducing/
Carbohydrates Type Units Linkage
Non Reducing

Glucose Monosaccharide Reducing Glucose —

Fructose Monosaccharide Reducing Fructose —

C1 of
a-D-Glucose
Glucose
Sucrose Disaccharide Non Reducing and b-D-
and C2 of
Fructose
Fructose

a-1, 4’
Both are
Maltose Disaccharide Reducing glycosidic
a-D-Glucose
linkage

b-D-Glucose a-1, 4’
Lactose Disaccharide Reducing and b-D- glycosidic
Galactose linkage

a-1, 4’
Amylose + and a-1, 6’
Starch Polysaccharide Non Reducing
Amylopectin glycosidic
linkage

b-1, 4’
Cellulose Polysaccharide Non Reducing b-D-Glucose glycosidic
linkage

a-1, 4’
and a-1, 6’
Glycogen Polysaccharide Non Reducing Amylopectin
glycosidic
linkage

Importance of Carbohydrates
y Carbohydrates are essential for life in both
plants and animals. They form a major portion
of our food.
Biomolecules

y Honey has been used for a long time as an


instant source of energy by ‘Vaids’ in ayurvedic
system of medicine.

18.
y Carbohydrates are used as storage molecules
as starch in plants and glycogen in animals. Concept Ladder
y Cell wall of bacteria and plants is made up of
cellulose.
Cellulose is commonly
y We build furniture, etc. from cellulose in
used in foods and bakery
the form of wood and clothe ourselves with
formulations as a source of
cellulose in the form of cotton fibre. They
dietary fiber or to improve
provide raw materials for many important
their texture. It is also used
industries like textiles, paper, lacquers and
as a bulking agent in low-
breweries.
calorie and gluten-free
baked products.
PROTEINS
y Brezeliues introduced the term protein which
means first (Proteios = first).
y Proteins are the most abundant biomolecules
of the living system. Chief sources of proteins
are milk, cheese, pulses, peanuts, fish, meat,
etc.
y They occur in every part of the body and
form the fundamental basis of structure and
functions of life. Rack your Brain
y They are also required for growth and
maintenance of body. What is the monomer unit of
y The word protein is derived from Greek word, protein?
“proteins” which means primary or of prime
importance.
y All proteins are polymers of α-amino acids.

Amino Acids
y Amino acids are carboxylic acids having
an –NH2 group. When the –NH2 group is at
α-position these are called α-amino acids.
NH2
|
R − CH − COOH Previous Year’s Questions
α-amino acid
Which of the following is a basic
y Depending upon the relative position of
amino acid?
amino group with respect to carboxyl group,
[NEET-2020]
the amino acids can be classified as α, β, γ, δ
Biomolecules

(1) Serine (2) Alanine


and so on. Only α-amino acids are obtained
(3) Tyrosine (4) Lysine

19.
on hydrolysis of proteins. They may contain
other functional groups also. Rack your Brain
y All α-amino acids have trivial names, which
usually reflect the property of that compound Lack of essential amino acids
or its source. in the diet leads to the disease
y Glycine is so named since it has sweet taste called?
(in Greek glykos means sweet) and tyrosine
was first obtained from cheese (in Greek,
tyros means cheese.)
y Amino acids are generally represented by a
three-letter symbol, sometimes one letter
symbol is also used. Structures of some
commonly occurring amino acids along with
their 3-letter and 1-letter symbols.

Classification of Amino Acids


y Amino acids are classified as acidic, basic or Concept Ladder
neutral depending upon the relative number of
amino and carboxyl groups in their molecule.
(1) Neutral : Equal number of amino and carboxyl Nonessential amino acids
groups makes it neutral support tissue growth and
(2) Basic : More number of amino than carboxyl repair, immune funciton,
groups makes it basic red blood cell formation,
(3) Acidic : More carboxyl groups as compared to and hormone synthesis.
amino groups makes it acidic.

Non-essential Amino Acids


y The amino acids, which can be synthesised in
the body, are known as nonessential amino
acids.

Essential Amino Acids


y Those which cannot be synthesised in the
body and must be obtained through diet, are
Previous Year’s Questions
known as essential amino acids.
y Their deficiency causes Kwashiorkor, a
disease. The non-essential amino acid
Examples of essential amino acids include, among the following is
valine, lucine, isolucine, lysine, threonil, phenyl [NEET-2019]
Biomolecules

alanine methionyl, tryptophan, histidine and (1) Lysine (2) Valine


arginine. (3) Leucine (4) Alanine

20.
Name of the Characteristic feature Three letter One letter
S.No.
Amino Acids of side chain. R symbol of code

1 Glycine H Gly G

2 Alanine —CH3 Ala A

3 Valine* (H3C)2CH— Val V

4 Leucine* (H3C)3CH—CH2— Leu L

5 Isoleucine* H3C − CH − CH − Ile I


|
CH3

6 Arginine* NH =C− NH − CH2


|
( )3 − Arg R
NH2

7 Lysine* (
H2N − CH2 )4 − Lys K

8 Glutamic acid HOOC—CH2—CH2— Glu E

9 Aspartic acid HOOC—CH2— AsP D

10 Glutamine O Glu Q
||
H2N − C− CH2 − CH2 −

11 Asparagine O Asn N
||
H2N − C− CH2 −

12 Threonine* H3C—CHOH— Thr T

13 Serine HO—CH2— Ser S


Biomolecules

21.
Name of the Characteristic feature Three letter One letter
S.No.
Amino Acids of side chain. R symbol of code

14 Cysteine HS—CH2— Cys C

15 Methionine* H3C—S—CH2—CH2— Met M

16 Phenylalanine* C6H5—CH2— Phe F

17 Tyrosine (p)HO—C6H5—CH2 Tyr Y

18 Tryptophan* Trp W

19 Histidine* His h

20 Proline Pro P

*Essential amino acids


Previous Year’s Questions
Charactertic Features of Amino Acids
y Amino acids are usually colourless, crystalline Which of the following comopund
solids. can form a zwitter ion?
y These are water-soluble and have high [NEET-2018]
melting point. (1) Aniline (2) Acetanilide
(3) Benzoic acid
Biomolecules

y These are behave like salts rather than simple


amines or carboxylic acids. This behaviour is (4) Glycine

22.
due to the presence of both acidic (carboxyl
group) and basic (amino group) groups in the Rack your Brain
same molecule.
Glycine exists as a zwitter ion
Zwitter Ion but o- and p-aminobenzoic
y In aqueous solution, the carboxyl group can acids not exists. Why?
lose a proton and amino group can accept a
proton, giving rise to a dipolar ion known as
zwitter ion.


y Zwitter ion is neutral but contains both
Concept Ladder
positive and negative charges.
y In zwitter ionic form, amino acids show
amphoteric behaviour as they react both with pH at which there is no
acids and bases. net migration of the amino
y Except glycine, all other naturally occurring acid under the influence of
α-amino acids are optically active, since an applied electric field is
the α-carbon atom is asymmetric. These called isoelectric point.
exist both in ‘D’ and ‘L’ forms. Most naturally
occurring amino acids have L-configuration.
L-Amino acids are represented by writing the
–NH2 group on left hand side.

Peptide bond or Peptide Linkage


Peptides are those amides which are formed
due to condensation between 2NH2 group
and–COOH group of two different amino
acids.
Previous Year’s Questions
y The –CO–NH– bond is called peptide linkage
or bond. The >C=O group of an amide is sp2
In a protein molecule various
hybridised with coplanar structure.
amino acid are linked together by
[AIPMT-2012]
(1) Peptide bond
(2) Dative bond
(3) a-glycosidic bond
Biomolecules

y The reaction between two molecules of


similar or different amino acids, proceeds (4) b-glycosidic bond

23.
through the combination of the amino group
of one molecule with the carboxyl group of Rack your Brain
the other. This results in the elimination of a
water molecule and formation of a peptide What is the peptide bond?
bond –CO–NH–. The product of the reaction
is called a dipeptide because it is made up of
two amino acids.
For example, when carboxyl group of glycine
combines with the amino group of alanine we
get a dipeptide, glycylalanine.

y An amino acid unit having a free NH2 group


is known as N-terminal amino acid while an
amino acid with a free –COOH group is known
as C-terminal amino acid.
y N-terminal amino acid residue in a protein
is determined by Sanger (1-fluoro-2,
4-dinitrobenzne) or DNP (2, 4-dinitrophenyl) Concept Ladder
method.
y C-terminal amino acid residue in a protein is
An alkaline solution of a
determined by hydrazinolysis.
protein or a polypeptide
y When writing the structure of peptides, the N
when treated with a
terminal end is taken on left hand side while,
few drops of 1% CuSO4
C-terminal end is at right hand side.
solution, produces a violet
colouration. The colour is
due to the formation of a
coordination complex of
Cu2+ with >C=O and -NH
groups.

y If a third amino acid combines to a dipeptide,
the product is called a tripeptide. A tripeptide
contains three amino acids linked by two
Biomolecules

peptide linkages.

24.
y When four, five or six amino acids are linked,
the respective products are known as Previous Year’s Questions
tetrapeptide, pentapeptide or hexapeptide,
respectively. When the number of such amino
In a protein molecule various
acids is more than ten, then the products are
amino acids are linked together
called polypeptides.
by
[AIPMT]
(1) peptide bond
(2) dative bond
(3) a-glycosiddic bond
(4) b-glycosidic bond

y A polypeptide with more than hundred amino
acid residues, having molecular mass higher
than 10,000 u is called a protein.

Classification of Proteins
Proteins can be classified into two types on
the basis of their molecular shape. Rack your Brain

(1) Fibrous Proteins What is snake venom made of?


y When the polypeptide chains run parallel and
are held together by hydrogen and disulphide
bonds, then fibre – like structure is formed.
y Proteins are generally insoluble in water and
are quite stable against a moderate change in
temperature and pH value.
Ex : keratin (present in hair, wool, silk) and myosin
(present in muscles), etc.
Concept Ladder
(2) Globular Proteins
y In such proteins, the polypeptide
intramolecular chains get folded to give Polypeptides are
a spheroidal shape due to intramolecular amphoteric in character
hydrogen bonding, van der Waals forces, because of the presence
dipolar interaction and disulphide bridging. of terminal ammonium and
These are usually soluble in water and change carboxylate ions as well as
with a change in temperature and pH. the ionized side chains of
amino acid residues.
Biomolecules

Ex : Insulin, ,albumins, Enzyme, haemoglobin and


antibodies.

25.
Hydrolysis of Proteins
Proteins can be hydrolysed and on the basis Previous Year’s Questions
of hydrolysis they are of following types.
(1) Simple Proteins : On hydrolysis they give only
Which is the correct statement?
a-amino acids
[AIPMT]
Ex :Albumins, globulins etc.
(1) Starch is a polymer of
(2) Conjugated Proteins : These are having a Non-
a-glucose
protein Prosthetic group and on it’s bases
(2) Amylose is a compoonent of
they are of following types.
cellulose
(a) Nucleo protein : Here Prosthetic group. is
(3) Proteins are comopsed of only
nucleic acid. e.g., Nuclein
one type of amino acid
(b) Glycoprotein : Here Prosthetic group is
(4) In cyclic structure of fructose,
any carbohydrate. e.g., Mycin
there are four carbons and one
(c) Chromo protein : Here Prosthetic group is
oxygen atom.
any pigment having metals like Fe, Cu, etc.
Ex : Haemoglobin, Chlorophyll.
(3) Derived Protein : They are achieved by the
partial hydrolysis of simple conjugated
proteins.
Ex : Proteoses, Peptones.
Structure of Proteins Rack your Brain
Amino acids are joined together by an amide
linkage called peptide bond. Proteins are long What is the disease caused by
polymers of amino acids linked by peptide defective heamoglobin molecule
bonds (polypeptides). in which one of the glutamic acid
(1) Primary Structure molecule is replaced by valine?
y Frederic Sanger gave Primary structure of
Insulin for the first time.
y Proteins may have one or more polypeptide
chains.
y Each polypeptide in a protein has amino acids Previous Year’s Questions
linked with each other in a specific sequence
and it is this sequence of amino acids that
The helical structure of protein is
is said to be the primary structure of that
stabilised by
protein.
[AIPMT]
(2) Secondary Structure (1) Dipeptide bonds
y The secondary structure arises due to (2) Hydrogen bonds
the regular folding of the backbone of the (3) Ether bonds
Biomolecules

polypeptide chain due to intramolecular (4) Peptide bonds


hydrogen bonding between the carboxyl and

26.
amino groups.
y They are found to exist in two different types Rack your Brain
of structures viz. α-helix and β-pleated sheet
structure. Which types of bonds are
y a-helix and b-pleated sheet structures arise responsible for the stability of
due to the regular folding of the backbone of a-helix?
the polypeptide chain due to hydrogen
O
bonding between || s and –NH– groups of
− C−

the peptide bond.

(a) a-Helix Structure


y α-Helix is one of the most common ways in
which a polypeptide chain forms all possible
hydrogen bonds by twisting into a right
handed screw (helix) with the –NH group of
each amino acid residue hydrogen bonded to
the >C=O of an adjacent turn of the helix.
y Stabilization of an α-helical configuration by
hydrogen bonding.
Ex : α-keratin in skin, nails, myosin in muscles,
fibroin in silk. α-Helix is called 3.6 helix as
each turn of helix has 3.6 amino acids and a
13-membered ring.

(b) b-pleated sheet structure


y In β-pleated sheet structure all peptide
chains are stretched out to nearly maximum
Biomolecules

extension and then laid side by side which


are held together by intermolecular hydrogen

27.
bonds.
y When the size of the groups (Alkyl Group) is
moderate, the polypeptide chains contract a
little to give a β-pleated sheet structure to
protein molecule, as in silk protein fibroin.
y β-pleated sheet structure are parallel and
Anti parallel type.
y In parallel form all polypeptide chain run in
the same direction while in Anti parallel form,
the alternate Polypeptide chain run in same
direction.
Ex : Parallel conformation — Keratin in hair
 Anti–Parallel Conformation — Silk Protein
fibroin

(3) Tertiary Structure


y The tertiary structure of proteins represents
the folding of the polypeptide chains or folding
Concept Ladder
of the secondary structure of proteins.
y Tertiary and secondary structures of proteins
are stabilise by the forces of H-bonds, The tertiary structure is
disulphide linkages, van der Waals and the three-dimensional
electrostatic forces of attraction. structure of globular
y It gives rise to two major molecular shapes proteins. It arises due
viz. fibrous and globular. to the folding and
superimposition of various
(4) Quaternary Structure secondary structural
y Some of the proteins are composed of two or elements.
more polypeptide chains referred to as sub-
units.
y The spatial arrangement of these subunits
with respect to each other is known as
quaternary structure. Previous Year’s Questions
Ex : Haemoglobin is an aggregate of four sub-units,
two identical α-chains (having 141 Amino acid Hemoglobin is
residues and two identical β-chains (having [AIPMT]
146 Amino acid residues). (1) A vitamin
(2) A carbohydrate
(3) An Enzyme
Biomolecules

(4) A globular protein

28.
Denaturation of Proteins
y Disruption of the native conformation of a
protein will cause the protein to loose its
biological activity. This is called denaturation.
y Various changes in the surroundings of a
protein such as pH, temperature, presence of
salts or certain chemical agents can disrupt
the complex three-dimensional structure Previous Year’s Questions
(conformation) of the proteins.
y Due to physical and chemical changes, the Which structure(s) of proteins
H-bonds are disturbed. remain(s) intact during
Ex :(i) 
On boiling an egg the albumin get denaturation process?
coagulated. [NEET-2019]
(ii) During formation of cheese from milk, (1) Both secondary and tertiary
the globular protein lactalbumin becomes structure
fibrous. (2) Primary structure only
Biomolecules

(3) Secondary structure only


(4) Tertiary structure only

29.
Detection of Protein
(1) Millon’s test: Aqueous solution of protein Concept Ladder
(except tyrosine) gives a white precipitate
with millon’s reagent (Mercurous nitrate and
The most widely used
mercuric nitrate in HNO2 ).
method for determining
(2) Xantho protein test: Here, protein having
the N-terminal amino acid
tyrosine and phenyl alanine amino acids give
residue in a protein or a
a yellow colour when tested with conc. HNO3
polypeptide molecule is
(3) Nin-hydrin test: Protein on boiling with
called the DNP-method or
dilute aqueous solution of nin-hydrin (2,
Sanger’s method.
4-dihydroxy indane-1, 3-dione) gives blue
violet colouration.
(4) Biuret test: Alkaline solution of proteins gives
violet colouration with 1% copper sulphate
solution due to formation of a complex
between Cu2+ and the peptide linkage.

LIPIDS
y Lipids are generally water insoluble.
y They could be simple fatty acids. A fatty acid Rack your Brain
has a carboxyl group attached to an R group.
The R group could be a methyl (–CH3), or ethyl
What is difference between lipid
(–C2H5) or higher number of –CH2 groups (1
and fat?
carbon to 19 carbons).
Ex : (i)  palmitic acid has 16 carbons
including carboxyl carbon.
(ii) Arachidonic acid has 20 carbon atoms
including the carboxyl carbon.
y Fatty acids could be saturated (without
double bond) or unsaturated (with one or
more C=C double bonds).
y Another simple lipid is glycerol which is
Previous Year’s Questions
trihydroxy propane.
y Many lipids have both glycerol and fatty acids.
The cell membranes are mainly
Here the fatty acids are found esterified with
composed of
glycerol. They can be then monoglycerides,
[AIPMT]
diglycerides and triglycerides.
(1) Fats
y These are also called fats and oils based on
(2) Proteins
melting point. Oils have lower melting point
(3) Phospholipids
Biomolecules

(e.g., gingelly oil) and hence remain as oil in


(4) Carbohydrates
winters.

30.
y Some lipids have phosphorous and a
phosphorylated organic compound in them.
These are phospholipids. They are found in
cell membrane. Lecithin is one example.
y Some tissues especially the neural tissues
have lipids with more complex structures.

ENZYMES
y Enzymes are biological catalysts which
increase the rate of biochemical reactions Concept Ladder
even under mild conditions of temperature
and pH of living organisms.
Iodine number is no. of
y Enzymes are chemically similar to globular
grams of I2 that combines
proteins.
with 100 g of fat or oil. It is
y Enzymes are very specific for a particular
used to measure extent of
reaction and for a particular substrate.
unsaturation in oil or fat.
y They are generally named after the compound
or class of compounds upon which they work.
Ex : The enzyme that catalyses hydrolysis of
maltose into glucose is named as maltase
Maltase
C12H22O11  → 2 C6H12O6
Maltose Glucose Previous Year’s Questions

y Sometimes enzymes are also named after the


Enzymes are made up of
reaction, where they are used.
[AIPMT]
Ex :The enzymes which catalyse the oxidation
(1) Edible proteins
of one substrate with simultaneous
(2) Proteins with specific
reduction of another substrate are named as
structure
oxidoreductase enzymes.
(3) Nitrogen containing
y The ending of the name of an enzyme is -ase.
carbohydrates
Biomolecules

y They are very specific in their action on


(4) Carbohydrates
substrates and each enzyme catalyses only a
specific type of reaction.

31.
y They are active at moderate temperature (310
K), neutral pH (7) and 1 atmospheric pressure. Concept Ladder
y The action of enzymes are inhibited by
various organic and inorganic molecules
Protein co-factor complex
called inhibitors.
is called holoenzyme while
y The activity of enzymes can be increased by
the inactive protein part is
metal ions and smaller organic molecules
apoenzyme.
called coenzymes or cofactors. For example,
Holoenzyme ⇌Apoenzyme
inorganic ions, Mg2+, Mn2+, Fe2+, Co2+, Cu2+ ,
+ cofactor
organic molecules like vitamins (thiamine,
riboflavin).

Mechanism of Enzyme Action


y Enzymes are needed only in small quantities
for the progress of a reaction.
y Enzymes function by lowering the energy of
activation of a particular reaction.
Ex : a
 ctivation energy for acid hydrolysis of
sucrose is 6.22 kJ mol–1, while the activation
energy is only 2.15 kJ mol–1 when hydrolysed Rack your Brain
by the enzyme.

which is cause of albinism?

Concept Ladder

Enzyme streptokinase is
used to dissolve blood clot
in coronary artery (which is
Biomolecules

cause of heart attack).

32.
Lock and Key Hypothesis
y A number of cavities are present on the Rack your Brain
surface of enzymes. These cavities have
specific shapes and groups like –NH2 –COOH, Urea’s enzyme can catalyse
–OH etc. hydrolysis of urea but not of
y These are active centres on enzyme surfaces. n-methyl urea. Why?
y Here ‘key’ (reagent or substrate) fits in the
‘lock’, that is, the active site of catalyst to give
an intermediate complex, which changes into
product and the enzyme catalyst is released.

R

E + S  
 E − S  → E +P
Activated
complex

S.No. Enzyme Enzymatic Reaction

(i) Invertase or sucrose Sucrose → Glucose + Fructose

(ii) Maltase Maltose → Glucose + Glucose

(iii) Lactose Lactose → Glucose + Galactose

(iv) a-Amylase Starch → n × Glucose

(v) Pepsin Proteins → a-Amino acids

(vi) Trypsin Proteins → a-Amino acids

(vii) Nucleases DNA or RNA → Nucleotides

(viii) DNA polymerase Deoxynucleotide triphosphates → DNA


Biomolecules

(ix) RNA polymerase Ribonucleotide triphosphates → RNA

33.
VITAMINS
y Those organic compounds are required in Definition
small amounts in our diet but their deficiency
causes specific diseases. These compounds organic compounds required
are called vitamins. in the diet in small amounts
y Most of the vitamins cannot be synthesised to perform specific biological
in our body but plants can synthesise almost functions for normal
all of them. maintenance of optimum
y Some of vitamins produce by bacteria of the growth and health of the
gut. organism.
y Vitamins are designated by alphabets A, B, C,
D, etc. Some of them are further named as
sub-groups e.g. B1, B2, B6, B12, etc.

Classification of Vitamins
y Vitamins are classified into two groups Rack your Brain
depending upon their solubility in water or
fat.
Which vitamin is not found in
plants?
(i) Fat Soluble Vitamins
y Vitamins which are soluble in fat and oils but
insoluble in water are kept in this group.
y These are vitamins A, D, E and K. They are Previous Year’s Questions
stored in liver and adipose (fat storing)
tissues.
Which of the following is not a
fat soluble vitamin?
(ii) Water Soluble Vitamins
[AIPMT-2011]
y Vitamins which are soluble in water but
insoluble in fat or oils. (1) Vitamin B complex
y B group vitamins and vitamin C are soluble in (2) Vitamin D
water so they are grouped together. (3) Vitamin E
(4) Vitamin A

Q4 Deficiency of which vitamin causes


(i) Pernicious anaemia (ii) convulsions

Sol. (i) Pernicious anaemia is caused by deficiency of vitamin B


(ii) Convulsion sare caused by deficiency of vitamin B .
.
12

6
Biomolecules

34.
S.No. Name of Vitamins Sources Deficiency diseases

Xerophthalmia (hardening
Fish liver oil, carrots,
(i) Vitamin A of cornea of eye) Night
butter and milk
blindness

Vitamin B1 Yeast, milk, green Beri beri (loss of appetite,


(ii)
(Thiamine) vegetables and cereals retarded growth)

Cheilosis (fissuring at
corners of mouth and
Vitamin B2 Milk, egg white, liver,
(iii) lips), digestive disorders
(Riboflavin) kidney
and burning sensation of
the skin.

Vitamin B6 Yeast, milk, egg yolk,


(iv) Convulsions
(Pyridoxine) cereals and grams

Meat, fish, egg and Pernicious anaemia (RBC


(v) Vitamin B12
curd deficient in haemoglobin)

Vitamin C Citrus fruits, amla and


(vi) Scurvy (bleeding gums)
(Ascorbic acid) green leafy vegetables

Rickets (bone deformities


Exposure to sunlight, in children) and osteo-
(vii) Vitamin D
fish and egg yolk malacia (soft bones and
joint pain in adults)

Vegetable oils like Increased fragility of


(viii) Vitamin E wheat germ oil, RBCs and muscular
sunflower oil, etc. weakness

Vegetable oils like


Increased blood clotting
(ix) Vitamin K wheat germ oil,
time
sunflower oil, etc.
Biomolecules

35.
NUCLEIC ACIDS
y Every generation of each and every species Concept Ladder
resembles its ancestors in many ways.
y It has been observed that nucleus of a living
Nucleic acids play
cell is responsible for this transmission of
an essential role in
inherent characters, also called heredity.
transmission of the
y The particles in nucleus of the cell, responsible
hereditary characteristics
for heredity, are called chromosomes which
and in the biosynthesis of
are made up of proteins and another type of
proteins.
biomolecules called nucleic acids.
y These are mainly of two types, the
deoxyribonucleic acid (DNA) and ribonucleic
acid (RNA). Since nucleic acids are long chain
polymers of nucleotides, so they are also
called polynucleotides.
y Nucleic acids contain the elements carbon,
oxygen, nitrogen, hydrogen and phosphorus.

Chemical Composition of Nucleic Acids


Rack your Brain
y Complete hydrolysis of DNA (or RNA) yields a
pentose sugar, phosphoric acid and nitrogen
What are the main function of DNA
containing heterocyclic compounds (called
and RNA in organisms?
bases).

Pentose Sugar
y In DNA molecules, the sugar moiety is β-D-2-
deoxyribose whereas in RNA molecule, it is
β-D-ribose.

Previous Year’s Questions



Deficiency of vitamin B1 causes
Bases
the disease
y The bases that occur in nucleic acids are
[AIPMT-2012]
derivatives of pyrimidine and purine.
(1) Convulsions (2) Beri-Beri
Biomolecules

(3) Cheilosis (4) Sterility

36.

y Pyrimidine bases are uracil, thymine and
cytosine.

y The purine bases found in nucleic acids are


adenine and guanine.

Previous Year’s Questions

In DNA, the linkages between


y DNA contains four bases viz. adenine (A), different nitrogenous bases are
guanine (G), cytosine (C) and thymine (T). [NEET-2013]
y RNA also contains four bases, the first three (1) Phosphate linkage
bases (adenine (A), guanine (G), cytosine (C)) (2) H-bonding
are same as in DNA but the fourth one is (3) Glycosidic linkage
Biomolecules

uracil (U). (4) Peptide linkage

37.
Chargaff Rule
y In 1955 Erwin Chargaff given the Chargaff Rack your Brain
Rule, according this rule in the DNA of any
given species, the ratio of adenine to thymine What is the chargaff rule and why
is equal, as is the ratio of cytosine to guanine. it is important?
This set of rules become known as Chargaff’s
ratio
y This rule was important for solving the
structure of DNA.
y Chargaff’s rule, [A] + [G] = [C] + [T]
y DNA from any species of any organism should
have a 1:1 stoichiometric ratio of purine and
pyrimidine bases.

Structure of Nucleic Acids


Nucleoside Previous Year’s Questions
y A unit formed by the attachment of a base to
1 position of sugar is known as nucleoside. in DNA, the linkages between
Sugar + Base = Nucleoside different nitrogenous bases are
y In nucleosides, the sugar carbons are [NEET-2013]
numbered as 1, 2, 3 etc. in order to distinguish (1) phosphate linkage
these from the bases. (2) H-bonding
(3) glycosidic linkage
Nucleotide (4) peptide linkage
y A nucleotide unit formed by the attachment
of a base 1 position of sugar and attachment
of phosphoric acid with 5 position of sugar.
Sugar + Base + Phosphoric acid = Nucleotide

y Nucleotides are joined together by


phosphodiester linkage between 5 and 3
Biomolecules

carbon atoms of the pentose sugar. The


formation of a typical dinucleotide.

38.
y A simplified version f nucleic acid chain is as
shown below.

Double strand helix structure for DNA


y The sequence of bases along the DNA or RNA
chain shows primary structures of these and
it controls the specific properties of nucleic
acids.
y An RNA molecule is usually a single chain of
ribose containing nucleotides.
y DNA consists of two long strands of Previous Year’s Questions
polynucleotides coiled around each other in
the form of a double helix (Watson and Crick Which of the following is correct
model) ladder like structure joint together by about H-bonding in nucleotide?
hydrogen bonding. [AIPMT]
y Here, hydrogen bonding is in between the (1) A-T, G-C (2) A-G, T-C
Biomolecules

nitrogenous base molecules of the nucleotide (3) G-T, A-C (4) A-A, T-T
monomer. Adenine with thymine forms two

39.
hydrogen bonds while guanine forms three
hydrogen bonds with cytosine. Rack your Brain
y Thymine combines only with deoxyribose
sugar while uracil combines with only ribose What type of linkage holds
sugar. together the monomers of DNA?

Concept Ladder

Mutation is sudden change


in base sequence of DNA
due to radiations or
chemicals.

Ribonucleic Acid (RNA)


y RNA single stranded helics is present which
sometimes foldsback on itself. Previous Year’s Questions
y RNA molecules are of three types and they
perform different functions.
The central dogma of molecular
y They are named as messenger RNA (m-RNA),
genetics states that the genetic
ribosomal RNA (r-RNA) and transfer RNA
information flows from
(t-RNA).
[NEET-2016]
(1) Amino acids → Proteins
Central Dogma
y Central Dogma was first proposed in 1958 by → DNA
Francis Crick, discoverer of the structure of
(2) DNA → Carbohydrates →
DNA.
Proteins
y Replication, Transcription, and Translation are
(3) DNA → RNA → Proteins
Biomolecules

the three main processes used by all cells


(4) DNA → RNA → Carbohydrates

40.
to maintain their genetic information and
to convert the genetic information encoded Definition
in DNA into gene products, which are either
RNAs or proteins, depending on the gene. A sequence of bases on DNA
is also unique for a person and
information regarding this is
called DNA fingerprinting.
Difference Between DNA and RNA

S.No. Deoxyribonucleic Acid (DNA) Ribonucleic Acid (RNA)

DNA occurs n the nucleus of the RNA occurs in the cytoplasm of the
(i)
cell. cell.

The sugar present in DNA is The sugar present in RNA is D-(–)-


(ii)
D-(–)-2-deoxyribose. ribose.

DNA contains cytosine and


RNA contains cytosine and uracil as
thymine as pyrimidine bases
(iii) pyrimidine bases and guanine and
and guanine and adenine as
adenine as purine bases.
purine bases.

DNA has double-standard RNA has single standard a-helix


(iv)
a-helix structure. structure.

RNA usually does undergo


(v) DNA undergoes replication.
replication.

DNA controls the transmission RNA controls the synthesis of


(vi)
of hereditary effects. proteins.

DNA Fingerprinting
y Dr. Khorana shared the Nobel Prize for
Medicine and Physiology in 1968 with Marshall
Biomolecules

Nirenberg and Robert Holley for cracking the


genetic code.

41.
y It is same for every cell and cannot be altered
by any known treatment. Concept Ladder
y DNA fingerprinting is now used
(i) in forensic laboratories for identification of
criminals. The process by which
(ii) to determine paternity of an individual. a single DNA molecule
(iii) to identify the dead bodies in any accident by produces two identical
comparing the DNA’s of parents or children. copies of itself is called
(iv)  to identify racial groups to rewrite cell division (mitosis) or
biological evolution. replication.

Biological Functions of Nucleic Acids


y A DNA molecule is capable of self-duplication
during cell division and identical DNA strands
are transferred to daughter cells.
y Proteins are synthesised by various RNA
molecules in the cell but the message for the Previous Year’s Questions
synthesis of a particular protein is present in
DNA. An example of biopolymer is
y DNA is the chemical basis of heredity and [AIPMT]
may be regarded as the reserve of genetic (1) teflon (2) neoprene
information. (3) nylon-6, 6 (4) DNA
y DNA is exclusively responsible for maintaining
the identity of different species of organisms
over millions of years.

The Major Complex Biomolecules of Cells

Biomolecule Building Block Major Functions

Protein Amino acid Basic structure and function of cell

DNA Deoxyribonucleotide Hereditary information

RNA Ribonucleotide Protein synthesis

Polysaccharide Monosaccharide Storage form of energy

Storage form of energy to meet long


Lipids Fatty acids & glycerol
Biomolecules

term demands

42.
HORMONES
y Hormones are molecules that act as Definition
intercellular messengers.
y Hormones are substances or biomolecules Hormones are produced by
manufactured in minute amounts in endocrine endocrine glands in the body
or ductless glands. and are poured directly in the
y They are carried directly into different parts blood stream which transports
by the blood stream. them to the site of action.
y The major hormone secreting glands include
the intestinal mucosa pancreas, adrenals,
thyroid, pituitary, ovaries and testes.

Types of Hormones
(1) Steroids
y Steroid hormones are produced by adrenal Concept Ladder
cortex and gonads (testes in males and
ovaries in females). If adrenal cortex does
Ex : estrogens and androgens. not function properly
y Hormones released by the adrenal cortex play then one of the results
very important role in the functions of the may be Addison’s
body. disease characterised
by hypoglycemia,
(i) Glucocorticoids weakness and increased
y Glucocorticoids control the carbohydrate susceptibility to stress.
metabolism, modulate inflammatory
reactions, and are involved in reactions to
stress.

(ii) Mineralocorticoids
y Mineralocorticoids control the level of
excretion of water and salt by the kidney. Previous Year’s Questions

(2) Polypeptids — e.g. insuline and endorphins. Which of the following hormones
is produced under the conditions
of stress which stimulate
(3) Amino Acids Derivatives — epinephrine and glycogenolysis in the liver of
norepinephrine.
human beings?
[NEET-2014]
(1) Thyroxin (2) Insulin
Biomolecules

(3) Adrenaline (4) Estradiol

43.
Functions of Hormones
y Hormones have several functions in the body. Rack your Brain
y They help to maintain the balance of biological
activities in the body. Which disease is caused by
y The role of insulin in keeping the blood glucose deficiency of insulin?
level within the narrow limit is an example of
this function. Insulin is released in response
to the rapid rise in blood glucose level.
y Hormone glucagon tends to increase the
glucose level in the blood. Insulin and
Glucagon hormones together regulate the
glucose level in the blood.
y Epinephrine and norepinephrine mediate
responses to external stimuli.
y Growth hormones and sex hormones play
role in growth and development.
y Thyroxine produced in the thyroid gland is an Previous Year’s Questions
iodinated derivative of amino acid tyrosine.
y Abnormally low level of thyroxine leads to Which of the following
hypothyroidism which is characterised by statements is not correct?
lethargyness and obesity. [NEET-2017]
y Increased level of thyroxine causes (1) 
Ovalbumin is a simple food
hyperthyroidism. reserve in egg-white
y Low level of iodine in the diet may lead to (2) Blood proteins thrombin and
hypothyroidism and enlargement of the fibrinogen are involved in
thyroid gland. This condition is largely being blood clotting.
controlled by adding sodium iodide to (3) Denaturation makes the
commercial table salt (“Iodised” salt). proteins more active.
y Hormones released by gonads are responsible (4) Insulin maintains sugar level
for development of secondary sex characters. in the blood of a human body.
y Testosterone is the major sex hormone
produced in males. It is responsible
for development of secondary male
characteristics (deep voice, facial hair, general
physical constitution).
y Estradiol is the main female sex hormone. It
is responsible for development of secondary
female characteristics and participates in the
control of menstrual cycle.
Biomolecules

y Progesterone is responsible for preparing the


uterus for implantation of fertilised egg.

44.
Organ of
S.No. Name Functions
Secretion

(A) Sex hormones

Control the development


(a) Androgens and normal functioning of
Testes
(Testosterone) Androsterone and male sex
organs.

Control the development and


(b) Estrogens (Estrone,
Ovary normal functioning of female sex
Estradiol, Estriol)
organs.

(c) Gestogens Corpus Control the development and


(Progesterone) luteum maintenance of pregance.

Adrenal cortex
Regulate the metabolism of fats,
hormones or
Adrenal proteins and carbohydrates;
(B) corticoids (Cortisone,
cortex control the balance of water and
Corticosterone,
minerals in the body.
Aldosterone etc.)

Organ of
Name Functions
Secretion

It is an amine compound and was the first


hormone to be isolated. Prepares animals
and humans for emergency in many ways by
raising the pulse rate, blood pressure etc.
(i) Adrenaline or Adrenal
stimulates the breakdown of liver glycogen
Epinephrine medulla
into blood glucose and fats into fatty acids
during emergency. These properties make
adrenaline as one of the most valuable drugs
used in medicine.

Thyroid Controls metabolism of carbohydrates, lipids


(ii) Thyroxine
gland and proteins.
Biomolecules

45.
Q5 Glucose or sucrose are soluble in water but cyclohexane and benzene (simple
six membered ring compounds) are insoluble in water Explain.

Sol. The solubility of a solute in a given solvent follows the rule ‘Like dissolves
like’. Glucose contains five and sucrose contains eight -OH groups. These -OH
groups form H-bonds with water.

Q6 What are the expected products of hydrolysis of lactose?

Sol. Lactose being a disaccharide gives two molecules of monosaccharides


one molecule each of D-(+)-glucose and D-(+)-galactose.
i.e.,

H O
C12H22O11  H2O 
3
or
 C6H12O6  C6H12O6
Lactose Lactose D (  ) Glucose D (  ) Glactose

Q7 The melting points and solubility in water of a-amino acids are generally higher
than those of corresponding halo acids. Explain.

Sol. a-amino acids as we all know, are dipolar in nature (N+H3–CHR–COO–) and
have strong dipolar interactions. As a result, these are high melting solids. These
are also involved in intermolecular hydrogen bonding with the molecules of
water and are therefore, water soluble. On the contrary, the halo acids RCH(X)
COOH are not dipolar like a-amino acids. Moreover, only the carboxyl group
of halo acids are involved in hydrogen bonding with the molecules of water
and not the halogen atoms. These have therefore, comparatively less melting
points and are also soluble in water to smaller extent.

Q8 Where does the water present in the egg go after boiling the egg?

Sol. When egg is boiled, proteins first undergo denaturation and then coagulation
and the water present in the egg gets absorbed in coagulated protein, probably
through H- bonding.

Q9 Why cannot Vitamin C be stored in our body?


Biomolecules

Sol. Vitamin C cannot be stored in the body because it is water soluble and is,
therefore, easily excreted in urine.

46.
Q10 Which products would be formed when a nucleotide from DNA containing
thymine is hydrolysed?

Sol. Upon hydrolysis, nucleotide from


phosphoric acid along-with thymine.
DNA would form 2-deoxyribose and

Q11 What are monosaccharides?

Sol. Monosaccharides are carbohydrates Which cannot be hydrolysed to smaller


molecules. Their general formula is (CH O)n Where n = 3 – 7 These are of two
2
types: Those which contain an aldehyde group (—CHO) are called aldoses and
those which contain a keto (C=O) group are called ketoses.

Q12 What are reducing sugars?

Sol. Reducing sugars are those which can act as reducing agents. They contain
in them a reducing group which may be aldehydic (-CHO) or ketonic (>C=0)
group.

Q13 Write two main functions of carbohydrates in plants.

Sol. Two major functions of carbohydrates in plants are following :


(a) Structural material for plant cell walls: The polysaccharide cellulose acts
as the chief structural material of the plant cell walls.
(b) Reserve food material: The polysaccharide starch is the major reserve food
material in the plants. It is stored in seeds and act as the reserve food
material for the tiny plant till it is capable of making its own food by
photosynthesis.

Q14 Classify
Biomolecules

the following into monosaccharides and disaccharides. Ribose,


2-deoxyribose, maltose, galactose, fructose and lactose.

47.
Sol. Monosaccharides: Ribose, 2-deoxyribose, galactose and fructose. Disaccharides:
Maltose and lactose.

Q15 What do you understand by the term glycosidic linkage?

Sol. The ethereal or oxide linkage through which two monosaccharide units
are joined together by the loss of a water molecule to form a molecule of
disaccharide is called the glycosidic linkage.

Q16 What is glycogen? How is it different from starch?

Sol. The carbohydrates are stored in animal body as glycogen. It is also called
animal starch and its structure is similar to amylopectin which means that it
is a branched chain polymer of a-D-glucose units in which the chain is formed
by C1—C4 glycosidic linkage whereas branching occurs by the formation of C1—
C6 glycosidic linkage. One main difference between glycogen and amylopectin
is the length of the chain.

Q17 What are the hydrolysis products of (i) sucrose, and (ii) lactose?

Sol. Both sucrose and lactose are disaccharides. Sucrose on hydrolysis gives one
molecule each of glucose and fructose but lactose on hydrolysis gives one
molecule each of glucose and galactose.
H O
C12O22O11  H2O 
3
 C6H12O6  C6H12O6
Sucrose D (  ) Glucose D (  ) Fructose
Biomolecules

H3O
C12O22O11  H2O 
 C6H12O6  C6H12O6
Lactose D (  ) Glu
ucose D (  ) Galactose

48.
Chapter Summary

1. Amino acids are organic compounds.


2. They are substituted methanes. The a-carbon has various substituents so they
are also called a-amino acids.
3. The a-carbon has an amino group, carboxylic group, hydrogen and a variable R
group. Based on the nature of the R group, there are 20 amino acids present in
proteins.
4. Amino acids can exist in a zwitterionic form, which changes according to the pH
of the solution to NH3+ (at low pH) or COO– (at high pH).
5. Primary Structure of protein is a long chain of amino acids in a specific sequence.
The amino acid chain starts from N’ and ends with C’. amino acids are linked by
C-N peptide bonds. The peptide bond is formed between the carboxyl (-COOH)
of one amino acid and amino group (-NH2) of another amino acid. The process of
peptide bond formation involves dehydration, one water molecule is released.
6. Secondary Structure of a protein has a helical structure. The long thread of amino
acids is folded right-handed to form a-helix or are arranged as b-pleated sheets,
which consist of b-strands, laterally joined by at least 2-3 hydrogen bonds.
7. Tertiary Structure of protein is highly folded. Protein chains are folded like a
hollow woollen ball. It is a three-dimensional organisation, which is required for
optimum activity.
8. Quaternary Structure is required when a protein is made up of more than one
polypeptide chain or has subunits. These spheres of subunits or polypeptides
may be arranged as linear strings or form a cube or plate. E.g. Haemoglobin
consists of 4 subunits, 2 subunits each of a and b type.
9. Carbohydrates are polymers of monosaccharides or simple sugars. They are the
main energy source of plants and animal cells. They have a general formula of
[Cx(H2O)y]n.
Biomolecules

49.
10. Reducing sugars- All monosaccharides are reducing sugar. Some disaccharides
are reducing, e.g. lactose, maltose, etc. They act as a reducing agent and reduce
Tollen’s, Fehling or Benedict’s reagents. They have free aldehyde or ketone group
(in a cyclic form hemiacetal or hemiketal group)
11. Non-reducing sugars- Sucrose (a disaccharide) is non-reducing as both the carbonyl
groups are involved in the glycosidic bond formation. All the polysaccharides
(cellulose, starch) are non-reducing.
12. Monosaccharides- Glucose, Galactose, Fructose, ribose, etc. They are the building
blocks of polysaccharides.
13. Disaccharides- They are the dimer of the same or different monosaccharides. The
monosaccharides are linked by a glycosidic bond between two carbons of the
monomers.
14. Maltose or malt sugar is made up of two a-D-glucose molecules linked by 1,4
linkage
15. Lactose is milk sugar and made up of b-D-galactose and b-D-glucose by 1,4
linkage
16. Sucrose is made up of glucose and fructose.
Biomolecules

50.

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