JEE (MAIN+ADVANCED)

BIOMOLECULES
 CONTENT

[Link] Pages

1. Biomolecules 01 – 46
2. Exercise-1 (Subjective Questions) 47
3. Exercise-2 (Objective Questions) 48 – 65
4. Exercise-3 (Section-A) 66 – 71
5. Exercise-3 (Section-B) 72 – 73
6. Exercise-4 74 – 76
7. Exercise-5 77 – 82
8. Answer Key 83 – 98
 B I O M O LE C U LE S

CARBOHYDRATES
Carbohydrates (hydrates of carbon) are naturallyoccuring 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
Cellulose and Starch (C6H10O5)n
Sucrose (Cane sugar) - C12H22O11, and Maltose (Malt Suger) C12(H2O)11
But some compounds which have formula according to Cx(H2O)y are not known as carbohydrate
Ex. CH2O Formaldehyde
C2(H2O)2 Acetic acid
C3(H2O)3 lactic acid

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)
C7H14O6 (Rahmnohexose)
Modern definition of carbohydrate: Carbohydrates are polyhydroxy aldehyde or ketone
or
Substances which yield these (polyhydroxyaldehyde or ketone)
on hydrolysis

Carbohydrates H/ H 2O
 Poly hydroxy aldehyde or ketone
Carbohydrates are also known as Saccharides.

CLASSIFICATION OF CARBOHYDRATES

Carbohydrates

Sugar Non Sugar (Polysacch.)

Sweet in taste, crystalline & soluble in water taste less, amorphous solid
(non crystalline) insoluble in
water
Monosaccharides Oligosaccharides These yields many sweet
monosacch. on acidic hydrolysis
Tetra (C6H12O5)n+nH2O  nC6H12 O6
Aldose Ketose Disacch. Trisacch.
Sucrose, maltose Refinose
lactose

Monosaccharides : (simple sugars)

These are the sugars which cannot be hydrolysed into smaller molecules. General formula is CnH2nOn .
Ex. - Glucose, Fructose, Ribose
Oligosaccharides :
These are the sugars which yields 2–10 monosaccharides units on hydrolysis. Such as.
(a) Disaccharides : Two monosaccharide unit on hydrolysis (may or may not be same).
Ex. - Sucrose, Maltose
(b) Trisaccharides : Three monosaccharide unit on hydrolysis.
Polysaccharides : These are the non sugars which yield a large no of monosaccharide units on
hydrolysis General formula - (C6H10O5)n. Ex.- Starch, Cellulose.
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 B I O M O LE C U LE S

Note :- Agroup of polysaccharides which are not so widely used in nature is pentosans (C5H8O4)n
Monosaccharides, General formula Cx(H2O)y x = 3 – 8. Nomenclature of monosaccharides are given
according to the no. of carbons present in them.

If –CHO group is present in monosaccharide, then it is known as aldose.

If  C  group is present in monosaccharide , then it is known as ketose.
||
O

Aldoses Ketoses
3C Tropose or Triose Aldotriose Ketotriose
4C Tetrose Aldotetrose Ketotetrose
5C Pentose Aldopentose Ketopentose
H C O

5C including –CHO Aldopentose (Ribose) H—C—OH

H—C—OH
H—C—OH
CH2 OH

5C including  C  Ketopentose (Ributose)

||
O

6C Hexose Aldohexose Ketohexose

CHO
|
H  C  OH
|
HO  C  H
|
6C including –CHO Aldohexose (Glucose) H  C  OH
|
H  C  OH
|
CH 2 OH

D  glucose

CH 2 OH
|
CO
|
HO  C  H
|
H  C  OH
6C including  C  Ketohexose (Fructose) |
|| H  C  OH
O |
CH 2 OH

D  fructose

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 B I O M O LE C U LE S

STEREOCHEMISTRY OF CARBOHYDRATES :

D & L-Sugars : 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 & L-sugars if it is towards
LHS.

Smallest carbohydrate Aldotriose CHO Glyceraldehyde

|
CH  OH
|
CH 2 OH

Fischer projection

Fisher formula of compounds containing manyasymmetric carbon.

a5 b5 a3 b3 CHO
a2 b2
CHO b3 a3
a4 b4
CH2OH b5 a5
a4 b4 a2 b2
CH2OH

Classification of Aldotetros : (i) Erythrose

(ii) Threoese
C-4

C-5

No. of C* = 3 (inAldopentose)
No. of optical isomers 23 = 8
No. of D Sugars 4
No. of L Sugars 4
D-Aldopentose :

All Isomeric D-sugars are diastereomers.

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 B I O M O LE C U LE S

Aldohexose :

No. of C* = 4
No. of stereoisomers = 24 = 16
No. of D-sugars = 8
No. of L-sugars = 8

The D–family aldoses

CHO
|
H  C  OH
|
CH 2OH

D-glyceraldehyde
CHO CHO
| |
H  C  OH HO C  H
| |
H  C  OH H  C  OH
| |
CH 2OH CH2OH

D-erythrose D-threose

CHO CHO CHO CHO

| | | |
H  C  OH HO C  H H  C  OH HO  C  H
| | | |
H  C  OH H  C  OH HO C  H HO  C  H
| | | |
H  C  OH H  C  OH H  C  OH H  C  OH
| | | |
CH 2OH CH2OH CH2OH CH 2OH

D-ribose D-arabinose D-xylose D-lyxose

CHO CHO CHO CHO CHO CHO

| | | | | | CHO CHO
H  C  OH HO  C  H H  C  OH HO  C  H H  C  OH HO  C  H | |
| | | | | | H  C  OH HO  C  H
| |
H  C  OH H  C  OH HO  C  H HO  C  H H  C  OH H  C  OH HO  C  H HO  C  H
| | | | | | | |
H  C  OH H  C  OH H  C  OH H  C  OH HO  C  H HO  C  H HO  C  H HO  C  H
| | | | | | | |
H  C  OH H  C  OH H  C  OH H  C  OH H  C  OH H  C  OH H  C  OH H  C  OH
| | | | | | | |
CH 2OH CH 2 OH CH 2OH CH 2 OH CH 2 OH CH 2 OH CH 2 OH CH 2OH

D() allose D() altrose D() glucose D( )mannose D()gulose D()idose D( ) galactose D() talose

Epimers: Apair of diastereomers that differ only in the configuration about of a single carbon atom are
said to be epimers. D(+)-glucose is epimeric with D(+)- mannose and D(+)-galactose as shown below.

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 B I O M O LE C U LE S

Epimers Epimers

CHO CHO CHO

| | |
H – C – OH H – C – OH HO – C – H
| | |
HO – C – H HO – C – H HO – C – H
| | |
HO – C – H H – C – OH H – C – OH
| | |
H – C – OH H – C – OH H – C – OH
| | |
CH2OH CH2OH CH2OH

D(+) galactose D(+) glucose D(+) mannose

C4 is epimeric carbon C2 is epimeric carbon

Another example with C2 epimeric carbon is

&

Anomers:Anomers are the stereoisomers which differs at a single chiral centre out of many & are ring
chain tautomer of the same open chain compound.
The two sugars that differs in configuration only on the carbon that was the carbonyl carbon in the open
chain form is called as anomers  glucose and  glucose are known as anomers their equilibrium mixture
contains 36 % –D–glucose , 63.8 % -D-glucose and 0.2 % open chain form.
C1 Carbon is known as anomeric carbon.

Haworth suggested to write  glucose and  glucose in pyran structure

O
CHO
HO H OH HO H
H
H HO HO H H OH
H O H OH HO H O
HO
H OH H OH
H OH
H H
CH2OH CH2OH CH2OH

D–glucose (open structure) –D–glucose

 –D–glucose
(sp rotation 112°) (sp rotation 19°)

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 B I O M O LE C U LE S

CH2OH CH2OH
O O
H H H H H OH
HO OH H OH HO OH H H
H OH H OH
Haworth formula Haworth formula
 –D–glucopyranose  –D–glucopyranose

Anomers are epimers but epimers may not be anomers.

CYCLIC STRUCTURES OF MONOSACCHARIDES

Many five membered and six membered monosaccharides occur in cyclic form. Cyclic structures of
monosaccharides are established by many experiments. The cyclic structure is due to intramolecular
hemiacetal formation between aldo / keto group and OH of any one carbon. The ring formed are
generally six membered (pyranose) or five membered (furanose). Each cyclization results in creation of
a new asymmetric centre apart from the existing ones. The isomers resulting from cyclizations are called
anomers. Example, when D-glucose (open structure) cyclise, it gives -D-glucose and -D-glucose.

Haworth projection :
Many of monosaccharides form cyclic structures. The actual structure is almost planer and be represented
by Haworth projection, which is a way of depicting three - dimensional cyclic structure.
Rule -1 : In a Haworth projection draw a fisher projection in which ring oxygen is in a down position.
Rule -2 : Imagine that carbon chain of fisher projection is folded around a barrel or drum, which
provide a ring lies in a plane  to the page.
Rule -3 : Now plane of ring is turned 90° so that anomeric carbon is on the right and the ring oxygen is
in the rear. Obtained projection is a Haworth projection.
Example : (D-glucose)
OH H
OH H H OH H
CHO OH CH2OH

CH2OH OH
CHO
H OH H OH
H
OH H

Projection :
H CH2OH H CH2OH
HO HO

H OH H O

H H
CHO
OH
OH OH
H
OH H OH H

Hawarth projection
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 B I O M O LE C U LE S

 Chair conformation of D–glucose

CH2OH
O H
H H
CH2OH H HO OH
HO H
H
O
H H
HO HO
HO H
OH
H
OH
Chair forms of (conformation) and  D-Glucose :
CH2OH
CH2OH O OH
OH OH
HO anomeric O
OH carbon
HO OH
OH
-D-Glucose (most stable glucose form) all groups are equatorial.
CH2OH
CH2OH O OH OH
HO anomeric O OH
HO carbon
HO OH
OH
-D-Glucose –OH group at anomeric carbon is axial.

Mutarotation

Specific rotation of  glucose + 112° Specific rotation of  glucose + 19°

Equilibrium mixture [ ]D = 52.5 degree mL g–1 dm–1

Fresh -glucose  52.5 Fresh -glucose

112° 36 %  glucose 19°
63.8 %  glucose
When pure -D glucose is dissolved in water its specific rotation is found to be +112° with time,
however the specific rotation of the solution decreases ultimately reaches stable value of +52.5°. When
 D-glucose is dissolved in water, it has a specific rotation of 19°. The specific rotation of this solution
increases with time also to + 52.5 °.
This change of optical rotation with time is called mutarotation. It is caused by the conversion of  and
 glucopyranose anomers into an equilibrium mixture of both. Mutarotation is catalyzed by both acid
and base, but also occurs is even in pure water. Mutarotation is characteristic of the cyclic hemiacetal
form of glucose.

Mutarotation occurs first by opening of the pyranose ring to the free aldehyde form.

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 B I O M O LE C U LE S

120°

Structure of fructose

CH2–OH HO–C–CH2OH
HOH2C–C–OH
C=O HO–C–H
HO–C–H O
O HO–C–H H–C–OH
H–C–OH  H–C–OH 
H–C–OH
H–C–OH
H–C–OH H–C
H–C
CH2–OH H
H
 fructose  fructose (more stable)

Ring structure of fructose C, Pyranose structures 6 membered ring, C2 – C6 linkage

H
H C O CH2OH
H
C H OH
OH C C OH
OH H
-D-fructopyranose -D-fructopyranose

Furanose structure (5 membered ring)

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 B I O M O LE C U LE S

Mutarotation: Fructose undergo complex mutarotation. The structure of the cyclic hemiacetal form of
d-fructose can be derived from it’s carbonyl (Ketone) form using the methods described as follows.

CH2OH
C=O
HO H CH2OH
H OH C=O
H OH HO H
CH2OH H OH
H OH This oxygen is
This structure is involved in
CH2OH
involved in pyranose furanose formation
formation

It happens that the crystalline form of D-fructose is -D-Fructopyranose. When crystals of this form are
dissolved in water, it equilibrates to both pyranose & furanose forms.

HO
H2C–C–OH HOH2C O OH O
anomeric HOH2C CH2OH
carbon
HOH2C–C–OH anomeric
HO–C–H O H HO
carbon
H CH2OH HO–C–H O H HO
H–C–OH H OH
H–C–OH
H–C OH H
H–C OH H
CH2OH  -D-fructofuranose
CH2OH  -D-fructofuranose
 -D-fructose

* All monosaccharides are reducing sugars, hence they show mutarotation.

* Starch, cellulose are Polymers of Glucose
* Lactose and sucrose are disaccharides
* Sucrose is a non reducing sugar, gives negative test for Benedict and tollen's reagent, they do not form
osazone and do not show mutarotation.
* Acetals of carbohydrates are called as GLYCOSIDE
FORMATION OF GLYCOSIDES

Glucose reacts with methyl alcohol in presence of dryHCl to form  and -methyl glycoside of glucose.
The reaction takes place only on OH of hemi-acetylic carbon. Other hydroxyl groups are unreactive.
H OCH3 CH3O H
C C
(CHOH)3 O (CHOH)3 O
CH CH
CH2OH CH2OH
 –Methyl glucose  –Methyl glucose

To methylate all the OH groups, methylating agent used is dimethyl sulphate.

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 B I O M O LE C U LE S

+ CH3OH HCl


Such compounds are called glucoside (cyclic acetals). They are special type of acetals in which one of
the oxygen of the acetal linkage is the ring oxygen of the pyranose or furanose.
H–C

Ring structure of glucose : H–C–OH

(i) Glucose does not give pink colour with schief reagent. HO–C–H O
(ii) Does not form adduct with NaHSO3, NH3 H–C–OH
(iii) Glucose exist in two isomeric form H–C
(iv) It show mutarotation CH2OH
Since there is no free aldehyde group, so it does not react with weak reagent (NH3, NaHSO3) but
strong reagent (HCN, NH2OH, C6H5NH – NH2) break up ring

Hydrolysis
  
H 2O


REACTIONS OF GLUCOSE

COOH
(CHOH)4 Br2 / H2O Red P / HI n Hexane
CH2OH or Alkaline
Gluconic acid solution of I2 CH3COCl
Pentaacetate
+
COONH 4 (5-OH group)
(CHOH)4 Tollen’s NH2–OH (1 eq)
C6H12O6 Oxime
Salts of CH2OH
gluconic acids HCN
COONa Glucose cyanohydrin
Fehling’s
(CHOH)4
5HIO 4
CH 2OH HCHO + 5HCOOH

COOH Schief's reagent, NaHSO 3

HNO3 No reaction
(CHOH)4 NH3
COOH
(Saccharic acid)

These reactions indicate that glucose has 6-C straight chain with one –CHO group & 5-OH group.
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 B I O M O LE C U LE S

GENERAL REACTIONS OF MONOSACCHARIDES

1. Acetylation :

+ 5CH3COCl / (CH3CO)2O  + 5HCl

This reaction suggests presence of 5( OH ) group.

Q. The penta acetate of glucose give –ve test with Tollen’s reagent & Fehling solution, explain?
No hemiacetal linkage, So no
CHO group in aq.
alkane solution –ve test
Tollen's –ve
Sol. 5
AcCl
 Fehling
–ve
Benedict
–ve
Shifts –ve
NaHSO3
–ve

2. Red by HI / Red P:

Re
dP / HI
 n-Hexane Re
dP / HI
 n-Hexane

3. Reaction with HCN:

+ HCN  + HCN 

4. Reaction with NH2–OH (hydroxyl amine):

+ NH2–OH  + NH2OH 

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 B I O M O LE C U LE S

5. Reaction with phenyl hydrazine: Both glucose and fructose give “osazone”.
Reaction with glucose :

+ 3 C6H5 NH – NH2  Osazone

Mechanism :

O O H
+ HC– N–NHPh
HC HC–NH2NHPh HC= N–NHPh 
HC–NH–NH–Ph
NH2NHPh IMPE
CHOH CH–OH CH–OH C – OH + +
–H2O –H C O H
R R R R
R
+
–H

HC=NNHPh HC=NH
2PhNHNH2
C NNHPh –NH3 C O

R R

Both compounds give same product because structure of last four C is same in both (glucose & fructose)
Only C-1 and C-2 in glucose and fructose are involved in osazone formation addition reaction do not
run through out the chain. The failure to undergo further reaction has been explained by stabilization of
the osazone by chelation.
Osazone :

or

So we do not get hexaphenyl hydrazone.

6. Catalytic reduction:

CH2OH CH2–OH

(CHOH)4 HO–C–H
H 2 / Ni or
  H 2 / Ni or
  D-sorbital + (CHOH)3
NaBH4 CH2OH NaBH4
D-sorbital CH2OH
D-Manitol
7. Oxidation:
Glucose Tollen
 's , Fehling
 Glucose dil
.HNO
3 
Br2 water

Glucose HIO
4  5HCOOH + HCHO + 5HIO3
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 B I O M O LE C U LE S

Oxidation of fructose :
Fructose Tollen
 's, Fehling

Fructose reduces tollen’s & fehling reagent because in basic medium fructose isomerises to glucose.
Fructose Br  No reaction
2 water


Fructose HNO
3  + +

8. Reaction with enzyme:

Glucose or Fructose Yeast
  2C2H5OH + 2CO2
Zymase enzyme

9. Lobery - de-Bryn-Von Ekanstein rearrangement

Glucose + Conc. NaOH  Yellow  Brown  Resin
(Resin is the mixture of lower sugars, HCHO and -hydroxy aldehyde)

Glucose Dil. NOH

Then there is a dynamic equilibrium
in glucose, fructose and mannose.
This is known as lobery de-bryne
von Ekanstein rearrangement

OH¯
Glucose Fructose

OH¯ Mannose OH¯

Here ene-diol mechanism takes place

H O H O–H
(A) CH2OH
C C
OH¯ (B) OH¯ C=O
H–C–O–H ene C–O–H (B)
diol (CHOH)3
(CHOH)3 (CHOH)3
CH2OH
CH2OH CH2OH
Fructose
OH¯ (A)

H O
C
OH – C – H

(CHOH)3
CH2OH
Mannose

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 B I O M O LE C U LE S

Epimerisation [The conversion of one epimer into another epimer]

The process of formation of epimer is called epimerisation
e.g. Glucose  Mannose

H O HO O HO O–H OH O
C C C C CHO
Br2 water Py Py  + 2H
H – C – OH H – C – OH C–O–H OH – C – H -lactose OH – C – H
Oxidation –CO2 Reduction
(CHOH)3 (CHOH)3 (CHOH)3 (CHOH)3 (CHOH)3
CH2OH CH2OH CH2OH CH2OH CH2OH
Gluconic acid Mannonic acid Mannose

Method of ascending the sugar series : An aldose may be converted into it’s next higher aldose eg.
an aldopentose into an aldohexose.
By Kiliani Fischer upgradation:

H 2Pd
HCN
   
aq. BaSO4 H
3O


Theoretically two lactones are possible, since two cyanohydrin may be formed when hydrogen
cyanide adds on to the aldopentose (a new assymetrical carbon is produced)

+ HCN  +

By Sowden reaction:

H
2SO 4


Mechanism :
H

 CH3OH + CH2 – NO 2 C=O 

CH 2 NO 2
| H 2SO 4
CH
3 H  C  OH 
OH   
 
|
Sowden has also stepped up an aldose to a ketose containing two additional carbon atoms using the
above method except that 2-nitroethanol is used instead of nitromethane.
CH 2 NO 2
+ | CH
3ONa
 H
2SO 4
 +
CH 2 OH

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 B I O M O LE C U LE S

Wolfrom reaction : Wolfrom have stepped up an aldose to a ketose with one more carbon
atom by a modifiedArndt-Eistere reaction.

Br
2  (
i ) Ac 2O
 CH
2N2
 (
i ) AcOH

H 2O ( ii ) SOCl 2 (ii ) Ba ( OH ) 2

Kochetkov reaction :
R
|
R CHOH
| |
CHOH Ph
3PCH COOEt
   CH OsO
4   Na
/Hg
 
HClO 4 
 HCl
|  Ph 3P O ||
CHO CH
|
COOEt

Method of descending the sugar series :

Wohl’s method:
CN
CHO CH=N–OH
CH–O–C–CH3 CHO
CHOH CHOH
NH2OH (CH3 CO)2O O aq. AgOH
(CHOH)3 + AgCN
(CHOH)3 (CHOH)3 excess (CH–O–C–CH3)3 
CH2OH
CH2OH CH2OH O
CH2 –O–C–CH3
O
Ruff’s method:

Br
2 /
H 2O
 Ca
salt
 + CO2
H 2O 2 / Fe 2 
Fenton 's
reagent

Conversion of an aldose into a ketose :

3
C6H 5 NHNH2
  HCl

 Zn
/ 
CH 3COOH
 

An aldehyde group is reduced more readily than a ketonic group.

Conversion of a Ketose into an aldose :

[
O]
 Na
/Hg
 
H
2 / Ni
 HNO3 
 HCl

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 B I O M O LE C U LE S

SOME IMPORTANT CARBOHYDRATES

1. Sucrose (C12H22O11) :  It is white, crystalline & sweet substance soluble in water obtained from the
sugar cane. When heated above its melting point, it forms a brown substance known as caramel.
It's aqueous solution is dextrorotatory [ ]D = 66.5°
dextro laevo
H+
C12H22O11 + H 2O C6H12O6 + C6H12O6
D-Glucose D-Frucose
 [D] = 52.7° []D = –92.4°

mixture is laevorotatory
(–)
Thus hydrolysis of sucrose brings about a change in the sign of rotation, from dextrol (+) to leavo (–) &
such a change is known as inversion of cane sugar and the mixture is known as invert sugar.
The inversion of cane-sugar may also be effected by the enzyme invertase which is found in yeast.
Sucrose is non-reducing sugar because it has stable acetal linkage & in aq. solution it can not give free
carbonyl group and so it does not reduces Tollen's & Fehling's solution.
This indicates that neither the aldehyde group of glucose nor the ketonic group of fructose is free in
sucrose.
anomeric C
6 1
CH2OH CH 2OH
O O
5 H
H H H 2 5
4 1 CH2OH
HO OH H O H HO
3 2 3 4
H OH HO H
–D–Glucopyranose –D–Fructofuranose

Structure of sucrose
(–D–glucopyranosyl– –D–fructofuranoside)

All non reducing sugars do not show mutarotation .

There is no free carbonyl group so it is non reducing sugar
-glycoside bond to anometric O
O CH2OH
position of D-glucose H
HOH2C
HO OH  linkage
HO CH2OH O at glucose
OH HO
HO OH O
HO O  linkage
O CH2OH H HO
b-Glycoside at fructose
bond to anomeric H CH2OH
positon of D-fructose CH2OH OH H

2. Maltose: It is obtained by partial hydrolysis of starch by the enzyme diastase present in malt i.e.,
sprouted barely seeds.
2 (C6H10O5)n + n H2O Diastase
  n C12H22O11
Starch Maltose
As stated above, hydrolysis of one mole of maltose yields two moles of D-glucose. Maltose is a reducing
sugar since it forms an osazone, undergoes mutarotation and also reduces Tollen’s and Fehling’s solutions,
Methylation studies have revealed that

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 B I O M O LE C U LE S

(i) both glucose units are present in the pyranose form.

(ii) C1 of one glucose unit is linked to C4 of the other
Further since maltose is hydrolysed by the enzyme maltase which specifically hydrolyses -glycosidic
linkage, therefore, the non-reducing glucose unit in maltose must be present in the -form. In other
words, C1 –  of non-reducing glucose unit is attached to C4 of the reducing glucose unit as shown in the
figure on next page.

3. Lactose (Milk sugar) C12H22O11

Lactose occurs in milk and that is why it is called milk sugar.
Lactose on hydrolysis with dilute acid or by enzyme lactase, yields an equimolar mixture of D-glucose
and D-galactose. It is a reducing sugar since it forms an osazone, undergoes mutarotation and also
reduces Tollen’s or Fehling’s solution. Methylation studies have revealed that
(i) both glucose and galactose are present in the pyranose form.
(ii) glucose is the reducing half while -galactose is the non-reducing half.
(iii) C1 of galactose unit is connected to C4 of glucose unit.

Further since emulsin, as, enzyme which specifically hydrolyses -glycosidic linkages also hydrolyses
lactose, therefore, galactose must be present in the -form. In other words, in lactose, C1 –  of galactose
is attached to C4 of glucose as shown in figure.

6
CH2OH
H O OH
5 
6 4 H
CH2OH OH H 1
HO O O 3 2
H
5

4 H H OH
OH H
H GLUCOSE
3 H (Reducing half)
2

H OH
GALACTOSE
(Non-reducing half)

4. Starch Amylum, (C6H10O5)n

Occurrence : The value of n (100 – 3000) varies from source to source. It is the chief food reserve
material or storage polysaccharide of plants and is found mainly in seeds, roots tubers etc. Wheat,
maize, rice, potatoes, barley, bananas and sorghum are the main sources of starch. Starch occurs in the
form of granules, which vary in shape and size depending upon their plant source.

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 B I O M O LE C U LE S

Occurs in all green plants. Starch consists of two fractions, one being known as –amylose, which gives
blue colour with iodine. This blue colour is believed to be due to the formation of an inclusion complex.
An aqueous solution of –amylose slowly forms a precipitate, since -amylose has a strong tendency to
'revert' to the insoluble state in solution. Amylopectin is insoluble in water and is stable towards both
hydrolysis to maltose by the enzyme diastase and to D(+)-glucose by dilute acids (amylopectin gives
about 50 percent of maltose).
6 6
CH2OH 6
CH2OH CH2OH
5 O O
H H H H 5 5 O
H H H H H
4 1 4 1
HO O O
4 1
OH H OH H
3 2 2
OH H OH
3 3 2
H OH H OH n–2 H OH
 –D–glucopyranose  –D–glucopyranose

Structure of Starch ( –D–glucoamylose)

–amylose consists of an unbranched chain, with a molecular weight varying between 10,000(n  60)
and 10,00,000(n  6,000), The value of n depends on the source and treatment of –amylose.
Properties : (i) Starch is a white amorphous powder sparingly soluble in water. Its aqueous solution
gives a blue colour with iodine solution due to the formation of an inclusion complex. The blue pears on
cooling.
(ii) On hydrolysis with dilute mineral acids or enzymes, starch beaks down first to smaller molecules
(n > n’), then to maltose and finally to D-glucose.

  H / H 2O
(C6H10O5)n H  (C6H10O5)n’ H/
/ H 2O
 C12H22O11 orMaltase
H 2O  C6H12O6
Starch Maltose D-Glucose
(iii) Starch is a non-reducing saccharide. It neither reduces Tollen’s reagent or Fehling’s solution nor
forms an osazone. This suggests that all hemiacetal OH groups of glucose units at C1 are not free but are
involved in glycosidic linkages.
Composition : Starch is not a single compound but is a mixture of two components–a water soluble
component called amylose (10-20%) and a water insoluble component called amylopectin (80-90%).
Both amylose and amylopectin are polymers of -D-glucose.

Structure of amylose :Amylose is water soluble and gives blue colour with iodine solution. It may have
100-3000 glucose units, i.e., its molecular mass can vary from 10,000 to 500,000. It is a linear polymer
of -D-glucose in which C1 of one glucose unit is attached to C4 of the other through -glycosidic
linkage as shown in figure.

Pectins
Pectins are found in plant and fruit juices. Their characteristic property is the ability of their solutions to
gelate, i.e. form jellies. Theyhave a high molecular weight and are polygalacturonic acid (linked 1,4) with
the carboxyl groups partially esterified with methanol.

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 B I O M O LE C U LE S

Glycogen (C6H10O5)n :
Glycogen is found in nearly all animals cells, occurring mainly in liver. It is the reserve carbohydrate of
animals and so is often known as 'animal starch'. It has also been isolated from plant sources.
Glycogen is a white powder, soluble in water, the solution giving a purplish-red colour with iodine. On
hydrolysis with dilute acid, glycogen gives D(+)-glucose. The molecular weight of glycogen has been
given as 10,00,000 to 50,00,000 and glycogen contains highly branched chains. Glycogen has a structure
similar to amylopectin, except that it has more cross-linking.
5. Cellulose:
Cellulose is colourless, solid which is insoluble in water & organic solvents. But it is soluble in ammonical
cupric hydroxide (Schweizer's reagent) or in conc. HCl cellulose is a regular polymer of d-glucopyranose
residues connected by -1,4 glycosidic linkages. It is straight chain polymer.
6 6
CH2OH CH2OH
5 O H 5 O
H H H
4 1 O 4 1 O
O OH
OH H H
3 2 H 3 2 H
H OH H OH
–D–glucopyranose –D–glucopyranose

Structure of Cellulose

Some points about cellulose :

1. General empirical formula (C6H10O5)

2. Cellulose + H2O H
 96% of crystalline D-glucose
3. No. of monomer units in cellulose are 1000 – 1500 in one molecule.
4. Cellulose doesn't show mutarotation (like starch)
5. It is non reducing sugar because there is no hemiacetal linkage.
6. Acetylations nitration & methylation of cellulose give trisubstituted cellulose which suggest that only three
– OH groups are free.

Tests for carbohydrates:

(i) When heated in a dry test tube, it melts, turns brown and finally black, giving a characteristic smell of
burning sugar.
(ii) When warmed with a little concentrated H2SO4, it leaves a charred reside of carbon.

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 B I O M O LE C U LE S

(iii) Molisch’s Test (named afterAustrian botanist Hans Molisch) is a sensitive chemical test for the presence
of carbohydrates, based on the dehydration of the carbohydrate by sulfuric acid to produce an aldehyde,
which condenses with two molecules of phenol (usually α-naphthol, though other phenols (e.g. resorcinol,
thymol) also give colored products) resulting in a red- or purple-colored compound.

The test solution is combined with a small amount of Molisch’s reagent (α-naphthol dissolved in ethanol)
in a test [Link] mixing, a small amount of concentrated sulfuric acid is slowly added down the sides
of the sloping test-tube, without mixing, to form a bottom layer. A positive reaction is indicated by
appearance of a purple ring at the interface between the acid and test layers.

All carbohydrates — monosaccharides, disaccharides, and polysaccharides — should give a positive

reaction, and nucleic acids and glycoproteins also give a positive reaction, as all these compounds are
eventually hydrolyzed to monosaccharides by strong mineral acids. Pentoses are then dehydrated to
furfural, while hexoses are dehydrated to 5-hydroxymethylfurfural. Either of these aldehydes, if present,
will condense with two molecules of naphthol to form a purple-colored product, as illustrated below by
the example of glucose:

BARFOED'S TEST
Barfoed's Test is a chemical test used for detecting the presence of monosaccharides. It is based on
the reduction of copper (II) acetate to copper (I) oxide (Cu2O), which forms a brick-red precipitate.
Barfoed's reagent consists of a 0.33 molar solution of neutral copper acetate in 1% acetic acid solution.
The reagent does not keep well and it is therefore advisable to make it up when it is actually required.
Reducing monosaccharides are oxidized by the copper ion in solution to form a carboxylic acid and a
reddish precipitate of copper (I) oxide within three minutes. Reducing disaccharides undergo the same
reaction, but do so at a slower rate and ppt. will come after 10 min. For Non reducing saccharides ppt.
will not form.
H O HO O
C +2 C +
+ 2 Cu + 2 H 2O + Cu2O + 4H
R R
The aldehyde group of the monosaccharide which normally forms a cyclic hemiacetal is oxidized to the
[Link] of other substances, including sodium chloride may interfere.

STARCH
Plants store glucose as the polysaccharide starch. The cereal grains (wheat, rice, corn, oats, barley) as
well as tubers such as potatoes are rich in starch.
Starch can be separated into two fractions--amylose and amylopectin. Natural starches are mixtures of
amylose (10-20%) and amylopectin (80-90%).

Iodine - KI Reagent: Iodine is not very soluble in water, therefore the iodine reagent is made by
dissolving iodine in water in the presence of potassium iodide. This makes a linear triodide ion complex
with is soluble. The triodide ion slips into the coil of the starch causing an intense blue-black color.

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 B I O M O LE C U LE S

Chemically, proteins are high polymers. They are polyamides and the monomers from which they are
derived are the - amino carboxylic [Link] protein molecule contains hundreds or even thousands
of amino acid units. These unitscan be of twenty-odddifferent kinds. Thenumberof different combinations,
i.e., the number of different protein molecules that are possible, is almost infinite.

1. Neutral amino acids (with nonpolar side chains)

ISOELECTRIC
NAME ABBREVIATIONS STRUCTURAL FORMULAE
POINT[pI]

@Glycine Gly(G) 6.0

Alanine Ala(A) 6.0

Valine* Val(V)
6.0

Leucine* Leu(L) 6.0


CH 3 N H 3
| |
Isoleucine* Ile(I) CH 3CH 2 CH  CHCO 2 6.0


N H3
|
Methionine* Met(M) CH 3SCH 2CH  CHCO 2 5.7

@@Proline Pro(P) 6.3

Phenylalanine* Phe(F) 5.5

Tryptophan* Trp(W) 5.9

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 B I O M O LE C U LE S

2. Neutral amino acids (with polar, but nonionized side chains)

NAME ABBREVIATIONS STRUCTURAL FORMULAE ISOELECTRIC

POINT[pI]

Asparagine Asn(N) 5.4

Glutamine Gln(Q) 5.7

Serine Ser(S) 5.7


Threonine* Thr OH N H 3
| | 5.6
CH 3CH  CHCO 2

Tyrosine Tyr(Y) 5.7


N H3
| 5.1
Cysteine Cys HSCH 2  CHCO 2
 
N H3 N H3
| |

| Cystine
Cys–Cys 
OOCCHCH 2S  SCH 2 CHCOO 

3. Acidic amino acids (side chain with carboxylic acid group)

ISOELECTRIC
STRUCTURAL FORMULAE POINT[pI]
NAME ABBREVIATIONS

Aspartic acid Asp(D) 2.8

GlutamicAcid Glu(E) 3.2

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 B I O M O LE C U LE S

4. Basic amino acids (side chain with nitrogenous basic group)

NAME ABBREVIATIONS STRUCTURAL FORMULAE ISOELECTRIC
POINT[pI]

Lystine* Lys(K)
9.7

Arginine* Arg(R)
10.8

Histidine* His(H)
7.6

AMINO ACIDS AND PROTEINS

NH 2
|
Bifunctional compounds R  CH  COOH having an acidic corboxylic group & a basic amino group.
There are 20 amino acids commonly found in proteins and are standard amino [Link] are  amino
acids. Most of them have 1° amino group.(– NH2). However proline is a 2° amino

CH2—COOH Me—CH—COOH Ph—CH2—CH—COOH N COOH

NH2 NH2 NH2 H

Proline [P]
(Gly) Glycine [G] Alanine [A] Phenyl alanine [F] Proline [P] (-imino acid)
All amino acids are chiral molecules with atleast one chiral carbon except glycine, H3NCH2COO¯.
All other amino acids are optically active & can be assigned D & L configuration.
\\\\\\\\\\\\\\\\\\\\

COOH COOH
H NH2 H2N H
CH3 CH3
D-Alanine L-Alanine

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 B I O M O LE C U LE S

Classification of Amino acids

Occurance Requirement Chemical Nature

Natural Essential Neutral
Synthetic Non Essential Acidic

Semi Essential Basic

Based on requirement
1. Essential amino acids can not be synthesized in human body so dietary intake is required. For any human
being 1 gm a day is required.
2. Semi essential amino acids can be synthesized in human body but dietary intake is required during
growing stages (when more of cell division is required).
For example : Early childhood, pregnancy and lactating mother.
3. Non essential amino acid - Body can synthesize them.

Chemical classification
Neutral - Amino acid having equal number of NH2 and COOH.
Neutral amino acids are further classified as polar and nonpolar depending on whether their side chains
have polar substituents (for example, asparagine with an NH2CO group) or are completely hydrocarbon
in nature (for example alanine, valine etc.).
Acidic -Amino acid having more COOH than NH2
Aspartic acid and glutamic acids, each with a second CO2H in their side chain are acidic amino acids.
Basic - Amino acid having more NH2 than COOH
Lysine, arginine and histidine, each with a basic site in their side chain are basic amino acids.

Proteins: The name protein is taken from the Greek word "proteios", which means "first". Of all
chemical compounds, proteins must almost certainly be ranked first, for they are the substance of life.
Proteins make up a large part of the animal body, they hold it together and they run it. They are found in
all livingcells.

Note :
* Amino acids with an asterisk are essential amino acids, that must be supplemented through diet.
| At pH = 7, Asp and Glu have a net negative charge and exist as anions. At pH = 7, Lys andArg have a
net positive charge and exist as cations. Rest of the amino acids at this pH exist in the neutral form.

| Structurally, in cystine, the two cysteine molecules are joined through sulfur (disulfide linkage).
@@ Proline is an -imino acid, all amino acids are primary amines except proline and 4-hydroxyproline,
which are 2° amines.
@ Except Glycine all other amino acids are optically active.

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 B I O M O LE C U LE S

Preparation of amino acids

(a) Gabriel Phthalimide synthesis
Better yields are generally obtained by the gabriel phthalimide synthesis ; the  - halo esters are used
instead of  - halo acids .

O O
C C
+ – KCl
N¯ K + Cl–CH 2COOC2H5 N– CH2COOC2H5
C C
O O
Potasium
phthalimide HCl , H2O

+
Cl¯ H3N – CH2 COOH + phthalic acid
Glycine hydrochloride

(b) Amination of  - Halo acids

Sometimes an  - chloro or  - bromo acid is subjected to direct ammonolysis with a large excess of
concentrated ammonia. For example.
Br2, P
CH3CH2COOH CH3CHCOOH NH3(excess) CH 3CHCOO¯
+
Br NH3
-Bromopropionic acid Alanine

(c) From diethyl malonate

COOC2H5 COOC2H5 COOH


C6H5 CH2Cl H3 O
Na+  CH HC– CH 2C 6H 5 H–C– CH2C6H 5

COOC2H5 COOC2H5 COOH

Sodiomalonic ester Ethyl benzylmalonate Benzylmalonic acid

Br2/ OH

COOH
NH3(excess) heat Br–C– CH C H
C6H5CH2CHCOOH C6H 5CH2CHCOOH 2 6 5
–CO2
NH3+ Br COOH
Phenylalanine
35% overall yield

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 B I O M O LE C U LE S

(d) Strecker's synthesis

Strecker's synthesis is also used for preparing  - amino acids

+
O N–H N–H NH2 NH2
+
–H2O CN¯ H2 O H3 O
R–C–H + NH3 R–C–H R–C–H R–C–H R–C–H
Imine
CN CN COO¯
 - amino nitrile  - amino acid
In this reaction general aldehyde is treated with mixture of ammonium chloride and KCN in aqueous
solution which forms NH3 and HCN, NH4Cl + KCN aqueous NH4CN + KCl,
NH4CN aqueous NH3 + HCN
(e) Using KOOP synthesis
Br NH NH2
O
HVZ DMSO NH3 SBH
CH3COOH CH2—COOH CH—COONa CH—COONa CH2
NaHCO3 Xs

COONa
Properties of Amino acids
Although the amino acids are commonly shown as containing an amino group and a carboxyl group,
H2NCHRCOOH, certain properties, (both physical and chemical) are not consistent with this structure
I. Physical properties
In contrast to amines and carboxylic acids, the amino acids are nonvolatile crystalline solids, which melt
with decomposition at fairly high temperatures.
They are insoluble in non-polar solvents like petroleum ether, benzene or ether and are appreciably
soluble in water.
Their aqueous solutions behave like solutions of substances of high dipole moment.
Amino acids as dipolar ions
Acidity and basicity constant are ridiculously low for –COOH and –NH2 groups. Glycine, for example,
has Ka = 1.6 × 10–10 and Kb = 2.5 × 10–12, whereas most carboxylic acids have Ka values of about
10–5 and most aliphatic amines have Kb values of about 10–4.
All these properties are quite consistent with a dipolar ion structure for the amino acids (I)
+
H3N–CH–COO¯
R
Amino acids : dipolar ions (Zwitter ion)

Physical properties - melting point, solubility, high dipole moment - are just what would be expected of
such a salt. The acid-base properties also become understandable when it is realized that the measured
Ka actually refers to the acidity of an ammonium ion, RNH3+,
+ +
H3NCHCOO¯ + H2O H3O + H2NCHCOO¯
R R
Acid
+
[H3O ] [H2NCHRCOO ]
Ka = +
[H3NCHRCOO¯]
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 B I O M O LE C U LE S

When the solution of an amino acid is made alkaline, the dipolar ion (I) is converted into the anion (II).
The stronger base, hydroxide ion, removes a proton from the ammonium ion and displaces the weaker
base, the amine.
+
H3NCHCOO¯ + OH¯ H2NCHCOO¯ + H2O
R (I) R (II)
Stronger Weaker Weaker
Stronger base acid
acid base

+
H
+
+ H +
H2NCHCOO¯ H3NCHCOO¯ H3NCHCOOH
OH¯ OH¯
R R R
(II) (I) (III)
Anion Ampholyte Cation

Wherever feasible, we can speed up a desired reaction by adjusting the acidity or basicityof the solution
in such a way as to increase the concentration of the reactive species.

Isoelectric point of amino acids

What happens when a solution of an amino acid is placed in an electric field depends upon the acidity or
basicity of the solution.
+
H
+
 H 
H2NCHCOO¯ H3NCHCOO¯ H3NCHCOOH
OH¯ OH¯
R R R
Ka 2 Ka 1
(II) A (I) DI (III) C

In quite alkaline solution, anions (II) exceed cations (III), and there is a net migration of amino acid
toward the anode. In quite acidic solution, cations (III) are in excess, and there is a net migration of
amino acid toward the cathode. If (II) and (III) are exactly balanced, there is no net migration ; under
such conditions any one molecule exists as a positive ion and as a negative ion for exactly the same
amount of time, and any small movement in the direction of one electrode is subsequently cancelled by
an equal movement back towards the other electrode. The hydrogen ion concentration of the solution
in which a particular amino acid does not migrate under the influence of an electric field is
called the isoelectric point (pI) of that amino acid. The isoelectric point (pI) is the pH at which
the amino acid exists only as a dipolar ion with net charge zero.
For glycine, for example, the isoelectric point is at pH 6.1.

An amino acid usually shows its lower solubility in a solution at the isoelectric point, since here there is
the highest concentration of the dipolar [Link] the solution is made more alkaline or more acidic, the
concentration of one of the more soluble ions, (II) or (III) increases.
[DI] [H  ] [A  ] [H  ]
Ka1 = Ka2 = at pI [ A ] = [C ]
[C  ] [DI]

[DI] [H  ] Ka 2 [DI]
Ka1
=
[H  ] [H  ]2 = Ka1 × Ka2

P Ka1  P Ka 2
on taking antilog pI =
2
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 B I O M O LE C U LE S

The pI of an amino acid that does not have an ionizable side chain. (e.g. alanine), is midway between its
two pKa values.
O

Alanine CH3–CH–C–OH pKa = 2.34


NH3 pKa = 9.69

2.34  9.69 12.03

pI = = = 6.02
2 2
If an amino acid has an ionizable side chain, its pIis the average of the pKa values of the similarlyionizing
groups (positive ionizing to uncharged or uncharged ionizing to negative.)
For example :

(i) Lysine
O pKa = 2.18

H3N –CH2 – CH 2 – CH2 – CH2 – CH – C – OH

pKa = 10.79 NH3 pKa = 8.95

10.79  8.95 19.74

pI =  = 9.87
2 2
(ii) Glutamic acid

O O pKa = 2.19
HO–C–CH2 – CH2 – CH – C – OH

pKa = 4.25 NH3 pKa = 9.67

21.19  4.25 6.44

pI =  = 3.22
2 2
An amino acid having more COOH than NH2 or more acidic COOH will have pI less than 7.
An amino acid having more – NH2 than COOH or more basic – NH2 will have pI more than 7.

Q. Write the structure of alanine at pH 2.5, 10.5 and 6.

Electrophoresis
The movement of charged molecules (like amino acid) under the influence of an electric field is called
electrophoresis. Electrophoresis separates amino acids on the basis of their pI values.
Amino acid is positively charged (moves towards cathode) if pH of the solution < pI
Amino acid is negatively charged (moves towards anode) if pH of the solution > pI

Q. How will you separate a ternary mixture of arginine, alanine & aspartic acid?
Ans. A few drops of a solution of an amino acid mixture are applied to the middle of a piece of filter paper.
When the paper is placed in a buffer solution (pH = 5) between the two electrodes and an electric field
is applied then arginine & alanine with pI > pH move towards the cathode and aspartic acid with pI < pH
moves towards the anode. Out of arginine & alanine, alanine will move slowly towards the cathode due
to lesser positive charge.

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Before electrophoresis
After electrophoresis
– +
– +

Buffer solution
(pH = 5) A B C
Buffer solution
(pH = 5)

Mixture of arginine
+ alanine + aspartic acid Figure (ii)
Figure (i)

A = arginine (pI = 10.76) B = alanine (pI = 6.02) C = aspartic acid (pI = 2.98)

NH2 O  
|| CH3CHCOO OOCCH2CHCOO
| |

H2NCNHCH2 CH2CH2 CHCO
NH3 NH3
|
NH3

General reactions of amino acids

(1) Reactions due to – NH2 group

H H
HBr  COOH
 COOH
 
NH3 Br
NH2 H CH2—COOH
MeCOCl PhCOCl
 COOH CH2—COOH
NHCOMe NH2
H NH—C—Ph
NaNO2
 COOH
HCl O
OH Hipuric acid
H
NOCl  COOH
Cl
H
NOBr  COOH
Br

H H
HCHO
 COOH  COOH Sorison's titration method.

NH2 N = CH2
Reactions is used to block – NH2 group during volumetric analysis in.

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(2) Reactions due to – COOH group.

H
H
 COOH ROH  COOR
H 
NH3
NH2 H
NaOH

CaO/
NH2
NaHCO3
Na salt

H
LAH  CH2OH
NH2
H
NH3  CONH2

NH2

(3) Heating Effect

(i) Heating of amino acids leads to intermolecular dehydration to form cyclic diamides.
O

CH2 –C–OH O
H
NH –2H2 O
NH NH N–H
H 
CH2
HO –C O

(ii) When alanine is heated, then two diastereomers are obtained. One of them (trans) is not resolvable.

O O
Me NH Me H NH Me

2MeCH(NH2)COOH –2H O +
2
NH H NH H
H Me
O O
Cis (Racemic) Trans (Meso)

(iii) When  - amino acids are heated, ,  - unsaturated salt are formed.

RCHCH2COOH RCH = CH–COONH 4

NH2

(iv)  - amino acids when heated alone gives  - lactam and polymer respectively. The reason for the
formation of polymer is that when  - amino cyclises intramolecularly, it leads to large angle strain within
the compound

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O O
O
O
OH Heat C– OH Heat
NH2 N–H + H2O N–H H2O N–H

- lactam H - lactam

  
NH3(CH2)5COO –NH(CH2)5–C –NH(CH2)5–C–NH(CH 2) 5C–

O O O
Nylon 6
(4) Peptide
Peptides are amides formed by interaction between amino groups and carbonyl groups of amino acids.
The amino bonds   NH  C   that link amino acid residues are called peptide bonds. So peptide
 || 
 O 
 
bonds are the only covalent bonds that hold amino acid residues together in a peptide or protein.
Depending upon the number of amino acid residues per molecule, theyare known as dipeptides, tripeptides
and so on and finally polypeptides. (By convention, peptides of molecular weight upto 1000 are known
as polypeptides and above that as protein)

O O O
  
H3N–CH2 –C–NH–CH2 COO H3N–CH2–C–NH–CH–C–NH–CH–COO
(Gly-Gly) CH3 CH2–Ph
Glycine-Alaninedipeptide (Gly-Ala-Phen Tripeptide)
Glycine-Alanine-phenylalanine

O O

H3N–CH–C–NH–CH–C—NH–CH–COO 
R R R
n
Polypeptide
Dipeptides are made from two amino acids where as oligopeptides are made from 3 to 10 amino acids.
If 11 to 100 amino acids are present together they called polypeptide and 100 onwards they are called
as macropeptide.

O O O O

H2N–CH2–C–OH + H2N–CH2–C–OH – NH–CH 2–C–NH–CH2–C –

n
+ peptide linkage
PhCOCl ROH/H
O O O O O

Ph–C–NH–CH2–C–OH H2N–CH2–C–OR Ph–O–C–NH–CH2–C–NH–CH2–C–OR

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For the synthesis of polypeptides, the amino groups that are not to be linked in peptide bonds must be
blocked so as to be unreactive. Then all other reactive functional groups must be protected to prevent
their participation in the coupling produces. The coupling must be effected by a method that does not
cause racemization or chemical alternation of the side chains.
These type polyamide can be made only using part blocking technique.
Abbreviated name of amion acid with free NH2 is written first.
By convention peptide are written with the free amino group (the –N–terminal amino acid) on the left
and the free carbonyl group (the –C– terminal amino acid) on the right.
O O

H3N–CH–C–NH–CH–C—O
R R’
For the nomenclature of peptides abbreviated name of amino acid with free NH2 group is written first.
For example:
O
H2N–CH2–C–NH–CH–COOH H2N–CH–CO–NH–CH2–COOH
CH3 CH3
(Gly-Ala) (Ala-Gly)
Glycine-Alanine-dipeptide Alanine-Glycine-dipeptide
Polypeptide on hydrolysis give two amino acid are known as dipeptide
O
HOOC –CH –NH–C–CH 2–NH 2 Dipeptide
Me
GlyAla [GlycineAlanine]
O O
H 2N–CH–C–NH–CH2–C–OH Ala - Gly [Alanine-Glycine ]
Me
Total number of polypeptide possible = Xn [X = type of amino acid interacting,
n = number of amino acid molecule are interacting.]
Q. Glycine can form how many Dipeptide ? [Ans. One]
Q. Glycine can form how manyTripeptide ? [Ans. One]
Q. Glycine andAla can form how many Dipeptide ? [Ans. Four]
Q. Gly,Ala, and PhenylAla can form how many Dipeptide ? [Ans. Nine]
Q. Gly,Ala, can form how manyTripeptide ? [Ans. Eight]

When Macropeptide takes different shape due to intramolecular H - bonding between different layers is
known as proteins

Proteins
You have already read that proteins are the polymers of -amino acids and they are connected to each
other by peptide bond or peptide linkage. Chemically, peptide linkage is an amide formed between —
COOH group and — NH2 group. The reaction between two molecules of similar or different amino
acids, proceeds through the combination of the amino group of one molecule with the carboxy1 group of
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 B I O M O LE C U LE S

the other. This results in the elimination of a water molecule and formation of a peptide bond — CO —
NH —. The product of the reaction is called a dipeptide because it is made up of two amino acids. For
example, when carboxy1 group of glycine combines with the amino group of alanine we get a dipeptide,
glycylalanine.
H2N — CH2 — COOH + H2N — CH — COOH

– H2O CH3

H2N — CH2 — CO — NH — CH — COOH

CH3
Peptide linkage

Glycylalanine (Gly-Ala)
If a third amino acid combines to a dipeptide, the product is called a tripeptide.A tripeptide contains
three amino acids linked bytwo peptide linkages. Similarly when four, five or six amino acids are linked,
the respective products are known as tetrapeptide, pentapeptide or hexapeptide, respectively. When
the number of such amino acids is more than ten, then the products are called [Link]
with more than hundred amino acid residues, having molecular mass higher than 10,000u is called a
protein. However, the distinction between a polypeptide and a protein is not very sharp. Polypeptides
with fewer amino acids are likelyto be called proteins they ordinarily have a well defined conformation
of a protein such as insulin which contains 51 amino acids.
Proteins can be classified into two types on the basis of their molecular shape.

(a) Fibrous proteins : When the polypeptide chains run parallel and are held together by hydrogen and
disulphide bonds, then fibre-like structure is formed. Such proteins are generally insoluble in water.
Some common examples are keratin (present in hair, wool, silk) and myosin (present in muscles), etc.

(b) Globular proteins : This structure results when the chains of polypeptides coil around to give a spherical
shape. These are usually soluble in water. Insulin and albumins are the common examples of globular
proteins.
Structure of Proteins
Structure and shape of proteins can be studied at four different levels, .i.e., primary, secondary, tertiary
and quaternary, each level being more complex than the previous one.

(i) Primary structure of proteins : Proteins may have one or more polypeptide chains. Each polypeptide
in a protein has amino acids linked with each other in a specific sequence and it is this sequence of amino
acids that is said to be the primary structure of the [Link] change in this primary structure i.e., the
sequence of amino acids creates a different protein.

(ii) Secondary structure of proteins : The secondary structure of protein refers to the shape in which a
long polypeptide chain can exist. They are found to exist in two different types of structures viz. -helix
and -pleated sheet structure. These structures arise due to the regular folding of the backbone of the
O
polypeptide chain due to hydrogen bonding between — C — and — NH — groups of the peptide
bond.

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R R''
CH C N CH
C N CH C N
O H R' O H
H O R' H O
N C CH N C
CH N C CH
R H O R''

-Flat sheet structure of a protein

-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 as shown in figure.
In -structure all peptide chains are stretched out to nearlymaximum extension and then laid side by side
which are held together, by intermolecular hydrogen bonds. The structure resembles the pleated folds of
drapery and therefore is known as -pleated sheet.

O N C H
C H O N
O H
C N
C N C
O H O
H O N C H
N C H O N

-pleated sheet structure of a protein

(i) Ionic bonding : between COO¯ and NH3+ at different sites.
(ii) H-bonding : mainly between side-chain NH2 and COOH, also involving OH's (Of serine, for example)
and the N–H of tryptophan.
(iii) Weakly hydrophobic Van der Waal's attractive forces engendered by side-chain R groups and
(iv) Disulfide cross linkages between loops of the polypeptide chain.
The same kind of attractive and repulsive forces responsible for the tertiary structure operate to hold
together and stabilize the subunits of the quaternary structure.

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H
H C
N
N O
C C
O O
H
N C
H O H
C N N
C A bigger helix
O O

-helix structure
(iii) Tertiary structure of proteins : The tertiary structure of proteins represents overall folding of the
polypeptide chains i.e., further folding of the secondary structure. It gives rise to two major molecular
shapes viz. fibrous and globular. The main forces which stabilise the 2° and 3° structures of proteins are
hydrogen bonds, disulphide linkages, van der walls and electrostatic forces of attraction.

\\\\\\\\\\\\\\\
\ \\\\\\\\\\\\\\\\\\\\\\\\\\\ \\\\\\\\\\\\ \
\\\ \ \\\ \\\\\\\\\\\\\\\\ \\ \ C \\\\\\\
CH O=C O
CH CH S O
3 3

CH3 CH3 S + H
CH NH3
\\\\\
\\\\\\\ \\\\\\\\\\\\\\\\\\\\ N \\\\\
\\\\\\\\\\\\\\\\\\\\\ Disulphide \\\\\\\\\\\\\\\\\\\\\\\\\\\\\\\\\
Hydrogen
Hydrophobic bond Salt
interactions bond
Bridge

Tertiary structure of proteins

(iv) Quaternary structure of proteins : Some of the proteins are composed of two or more polypeptide
chains referred to as sub-units. The spatial arrangement of these subunits with respect to each other is
known as quaternary structure.
According the their biological action, they are classified as enzymes, hormones, antibodies, etc.

N
O R H H
O
C CH N
N C CH C
H O R
Primary
Secondary

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Tertiary Quaternary

Diagrammatic representation of primary, secondary, tertiary and quaternary structure of protein

Denaturation of proteins
The process that brings about changes in physical as well as biological properties of proteins is called
denaturaion of protein.
Important features:
(a) It is caused by change in pH, temperature or by other denaturing agent like acid, alkali etc.
(b) Denaturation does not change the primary structure of protein but the secondary & tertiary structure.
(c) Denatured proteins lose its biological activity.
(d) During denaturation ordered and specific conformation convert into uncoiled and random conformation,
so entropy increases during denaturation.
(e) Denaturation may or may not be reversible.

TESTS OF PROTEINS

Biuret test : Addition of a very dilute solution of CuSO4 to an alkaline solution of a protein is done. A
positive test is indicated by the formation of a pink violet to purple violet color.
The name of test is derived from a specific compound, biuret, which gives a positive test with this reagent
O O
H2N—C—NH—C—NH2
biuret
When a protein reacts with copper (II) sulphate (blue), the positive test is the formation of a violet
colored complex.
H
O H
N N
R O
CH—C—N— + Cu+2 Cu
H (Blue)
N N
O H
H
(Violet)

The biuret test works for any compound containing two or more of the following groups.
O O NH S
—C—NH— —C—NH 2 —CH2—NH2 —C—NH 2 —C—NH2

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Ninhydrin Test : The ninhydrin test is a test for amino acids and proteins with a free –NH2 group.
Amino acids are detected byninhydrin [Link] amino acids give violet - coloured product with ninhydrin
(triketo hydroindene hydrate) except proline and 4 - hydroxy proline, which gives yellow colour with it.

When such an –NH2 group reacts with ninhydrin, a purple-blue complex is formed.

O O
O
R O
OH
H2N—CH—C—OH + 2 N
OH
O
O
O
(Purple-Blue)

The same violet coloured dye forms from all  -AA's with 1° amino groups because only their nitrogen
is incorporated into it. The 2° amines proline and 4 - hydroxyproline give different adducts that absorb
light at a different and thus have a different yellow colour.

Test for proteins

(1) Xanthoprotenic Test : This test is given by protein containing tyrosine or typtophase.
Protein conc
 .HNO3
 yellow colour NaOH
 orange colour

(2) Hellers Test : This test is commonly employed for detecting albumin in urine. When concentrated
HNO3 is poured along side of test tube containing protein solution, a white ppt. is obtained.

(3) Millon's Test : Millon's reagent is a mixture of mercurous and mercuric nitrates proteins containing
tyrosine give a white ppt. turning red when treated with Millon's reagent.

ENZYMES

General nature of enzymes

Enzymes are biological catalysts which bring about chemical reactions in living cells. Theyare produced
by the living organism, and are usuallypresent in only very small amounts in the various cells (about 0.01
percent). They can also exhibit their activity even when they have been extracted from their source. All
enzymes are globular proteins, many have been identified and a large number have been obtained in
crystalline form.

Nomenclature and classification

A common method of naming enzymes is add the suffix as to the name of the substrate, i.e., the substance
being acted upon, e.g., esterase acts on esters, amylase on starch (amylum), protease on proteins,
urease on urea etc. Some enzymes, however, have retained their trivial names e.g., emulsin, pepsin,
trypsin etc. Names are also used for particular enzymes, e.g., urease, amylase, or as general names for
groups of enzymes e.g., esterases, proteases etc.

Enzymes are divided into six main groups according to the nature of the reaction that is catalysed, and
each main group is given a code number. The main groups are :
1. Oxidoreductases : The enzymes catalyse oxidation-reduction reactions, and include oxidases (direct
oxidation with molecular oxygen), dehydrogenases (removal of hydrogen from substrates), etc.

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2. Transferases : This group of enzymes catalyses the transfer of various functional groups, e.g.,
transaminase.

3. Hydrolases : These catalyse hydrolytic reaction, e.g., proteases (Proteins), esterases (esters), etc.

4. Lyases : There are two types of lyases, one which catalyses addition to double bonds and the other
which catalyses removal of groups and leaves double bonds.

5. Isomerases : These catalyse various types of isomerisation, e.g., racemizes, epimerases, etc.

6. Ligases : These enzymes catalyse the formation of a bond between two molecules and is accompanied
by the breaking of a pyrophosphate bond ofATP or similar triphosphate.

Cofactors

Many enzymes require the presence of non-protein compounds in order to perform their catalytic action.
These compounds are collectively known as cofactors or activators, and fall into three main groups.
Coenzymes are organic molecules which may be separated from the enzyme by, e.g., dialysis. On the
other hand, some cofactors are bound to the enzyme and then referred to as the prosthetic group of its
enzyme. Finally, cofactors may be inorganic ions. In some cases the metal is tightly bound to the enzyme
which is then referred to as a metalloenzymes. In other case the enzymes are 'metal-activated'. Metal
activators are uni- or bi-valent metal cations e.g., Na+, K+, Mg2+, Zn2+, Ca2+.

The complex, enzyme-cofactor, is known as a holoenzyme, and when the cofactor has been removed
the protein that remain is known as an apoenzyme. This has no enzymic activity.

Some enzymes are synthesised in the organism in an inactive form; this is known as a zymogen.

Thus, e.g., the enzymes pepsin is synthesised as its zymogen, pepsinogen. This is converted into pepsin
in the presence of hydrochloric acid.

Coenzymes and prosthetic groups generally act as carriers of specific functional groups or specific
atoms. In order to act in this manner, these cofactors must exist in two forms, one form being converted
into the other during catalysed reaction, and the latter being reconverted into the former by a coupled
reaction. These two reaction may, or may not, follow each other.

(a) Nicotinamide-adenine dinucleotide (NAD+)

(b) Nicotinamide-adenine dinucleotide phosphate (NADP+)
(c)Adenosine triphosphate (ATP)

Specificity of enzyme action

One of the most characteristic properties of enzymes is their specificity of action. This specificity may be
manifested in one of three ways :

(i) An enzymes may catalyse a particular type of reaction, e.g., esterases hydrolyse only esters. Such
enzyme are said to be reaction specific. On the other hand, an enzyme may be specific for a particular
compound or class of compounds. These enzymes are substrate specific, e.g., urease hydrolyses only
urea; phosphatases hydrolyse only phosphate esters.
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(ii) Manyenzymes exhibit a kinetic specificity, e.g., esterases, although hydrolysis all esters, hydrolyse
the various esters at different rate; pepsin hydrolyses the peptide link, but is most active for those links
in which, among other things, the amino group belongs to an aromatic amino-acid and the carboxyl
group is one of a dicarboxylic amino-acid.

(iii) Manyenzymes are stereospecific, e.g., maltase hydrolyses -glycosides but no -glycosides, whereas
emulsin hydrolysis the latter but not the former.

It should be noted, however, that a given enzyme can exhibit more than one of the specificities, e.g.,
esterases, while hydrolysing only esters, may also hydrolyse one enantiomer (of an optically active ester)
more rapidly than the other.

Enzyme inhibitors

Enzyme activity can be reduced or inhibited by the presence of a various compounds. There are two
major types ofinhibition : competitiveand irreversible. Incompetitiveinhibition, theinhibitoris acompound
whose structure and geometrycloselyresemble that of the normal substrate. Competition occurs between
the two (for the active site), but inhibition can be reversed by increasing the concentration of the normal
substrate. It therefore follows that the enzyme inhibitor complex readily regenerates the two molecules in
competitive inhibition. On the other hand, in irreversible inhibition the inhibitor forms a highly stable
enzyme-inhibitors complex (via a covalent bond), and if sufficient inhibitor is present, the catalytic effect
of the enzyme towards its normal substrate is completely lost.

Classification of Vitamins:-
Vitamins are classified into two groups depending upon their solubility in water or fat.

(i) Fat soluble vitamins: Vitamins which are soluble in fat and oils but insoluble in water are kept in this
group. These are vitamins A, D, E and K. They are stored in liver and adipose (fat storing) tissues.

(ii) Water soluble vitamins: B group vitamins and vitamin C are soluble in water so they are grouped
together. Water soluble vitamins must be supplied regularly in diet because they are readily excreted in
urine and cannot be stored (except vitamin B12) in our body.
Some important vitamins, their sources and diseases caused by their deficiency are listed in Table.

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[Link]. Name of Vitamins Sources Deficiency diseases

Fish Liver oil, carrots, Xerophthalmia (hardening of

1 Vitamin A
butter and milk cornea of eye) Night blindness

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

2 Vitamin B1 (Thiamine)
vegetables and cereals retarded growth)

Cheilosis (fissuring at corners of

Vitamin B2 Milk, eggwhite, liver,
3 mouth and lips), digestive
(Riboflavin) Kidney
disorders and burning sensation
of the skin
Vitamin B6 Yeast, milk, egg yolk,
4 Convulsions
(Pyridoxine) cereals and grams
Pernicious anaemia (RBC
5 Vitamin B12 Meat, fish, egg and curd
deficient in haemoglobin)
Vitamin C Citrus fruits, amla and
6 Scurvy (bleeding gums)
(Ascorbic acid) green leafy vegetables
Rickets (bone deformitties in
Exposure to sunlight, fish children) and osteomalacia
7 Vitamin D
and egg yolk. (soft bones and joint pain in
adults)
Vegetable oils like wheat Increased fragility of RBCs and
8 Vitamin E
germ oil, sunflower oil, etc. muscular weakness

9 Vitamin K Green leafy vegetables Increased blood clotting time.

NUCLEIC ACIDS

The particle in nucleus of the cell responsible for heredity, are called chromosomes which are made up of
proteins and another type of biomolecules called nucleic acids.

These are mainly of two types

(1) Deoxyribonucleic acid (DNA)
(2) Ribonucleic acid (RNA)

DNA was first isolated in 1869 from the nucleic of white blood cells. Because this material was found in
the nucleus and was acidic, it was called nucleic acids.

Nucleic acids are long chain polymers of nucleotides, so they are also called polynucleotides.

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Nucleotide

Nucleoside Phosphoric acid

Pentose sugar Nitrogen base

-D-ribose (in RNA) Purine

-D-2-deoxyribose (in DNA) Pyrimidine

Nucleoside = Base + Sugar

Nucleoside = Base + Sugar + Phosphate
Complete hydrolysis of DNA(or RNA) yields a pentose, sugar, phosphoric acid and nitrogen containing
heterocylic compounds (called bases).
Nitrogen bases
Purine Pyrimidine

2 ring structure Single ring structure

2 rings are Pyrimidine ring (2N + 4C)
Pyrimidine ring (2N + 4C)
Imidazole ring (2N + 3C)
6 7 4
1N 5 N 3N 5
8
2 N 4 N 2 N 6
3 9 1
eg. : Adenine (A), Guanine (G) eg.: Thymine (T), Uracil (U), Cytosin (C)

DNA contains four bases viz. adenine (A), guanine (G), cytosine (C) and thymine (T). RNA also contains
four bases, the first three bases are same as in DNA but the fourth one is uracil (U).
NH2 O NH2
N C N C C
C C C NH HC N
HC HC
C CH C C HC C
N N N N NH2 N O
H H H
Adenine (A) Guanine (G) Cytosine (C)

O O
H3C C C
C NH HC NH
HC C HC C
N O N O
H H
Thymine (T) Uracil (U)

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Thymine and uracil differ only bya methyl group thymine is 5-methyl uracil.

All nitrogen bases are aromatic.

DNA molecules, the sugar moiety is -D-2-deoxyribose (D-ribose without an OH group in the 2-
position) whereas in RNA molecule, it is -D-ribose.

5 5'
HOH2C O OH HOH2C O OH
4 1 4 1
H H3 2H H H H3 2H H
OH OH OH H
-D-ribose -D-2-deoxyribose

Structure of Nucleic Acids

Nucleic acids are chains of five membered-ring sugars linked byphosphate groups. The anomeric carbon
of each sugar is bonded to a nitrogen of a hetero cyclic compound in a -glycosidic linkage ( linkage
is one in which the substituents at C-1 and C-4 are on the same side of furanose ring)

Phosphoric acid links the sugar in both RNA and DNA. The acid has three dissociable OH groups.
Each of the OH groups can react with an alcohol to form a phosphomonoester, a phosphodiester or a
phosphotriester. In nucleic acids, the phosphate group is a phosphodiester.
O O O O
P P P P
HO OH OH HO OH OR RO OH OR RO OR OR
Phosphoric acid Phosphomonoester Phosphodiester Phosphotriester

The purines and pyrimidines are bonded to the anomeric carbon of the furanose ring, purines at N-9 and
pyrimidines at N-1 in a -glycosidic linkage.

A compound containing a base bonded to D-ribose or to 2 deoxy-D-ribose is called a nucleoside.

A nucleotide is a nucleoside with either the 5' or the 3'-OH group bonded in ester linkage to phosphoric
acid. The nucleotides of RNA are called ribonucleotides while the nucleotides of DNA are called
deoxyribonucleotides.

O
5' 5'
HO – H2C O Base O – P – O – H2C O Base
4' 1' 4' 1'
2'H
O¯ 2'H
H H3' H H H3' H
OH OH OH OH
(a) (b)
Structure of (a) a nucleoside and (b) a nucleotide

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 B I O M O LE C U LE S

O base O base
O a -glycosidic O a -glycosidic
linkage linkage

2'-OH group
O OH O

O = P – O¯ O = P – O¯

O base O base
O O

O OH O
O = P – O¯ O = P – O¯

O base O base
O O

O OH O

RNA DNA

Sequence of RNA and DNA molecule

In nucleic acids, nucleotide subunits linked by phosphodiester bonds. These linkage join the 3' OH
group of one nucleotides to 5' OH group of next nucleotide. A dinucleotide contains two nucleotide
subunits, an oligonucleotide contains three to ten subunits, and a polynucleotide contains many subunits.
DNA and RNA are polynucleotides. The nucleotide at one end of the strand has an unlinked
5'-triphosphate group and the nucleotide at the other end of the strand has an unlinked 3'-hydroxyl
group.

5' end of chain

O O
5'
– O – P – O – CH2 O Base – O – P – O – CH2 O Base
O¯ Sugar O¯ Sugar

3'
OH O
Phosphodiester
– O– P = O
linkage
+ O
O 5' CH2 O Base
– O – P – O – CH2 O Base Sugar
O¯ Sugar 3'
OH
3' end of chain
OH

Formation of a dinucleotide

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 B I O M O LE C U LE S

A C G
3' 3' 3'

P P P OH
5' 5' 5'
a trinucleotide

Nucleic acids have both primary and secondary structure. The primary structure of a nucleic acid is the
sequence of bases in the strand.

Base Base Base

– Sugar – Phosphate – Sugar – Phosphate – Sugar –

n
Watson and Crick gave a double strand helix structure for DNA.
Two strands of DNAare helically coiled like a revolving ladder.
They concluded that DNA consists of two strands of nucleic acids with the sugar phosphate backbone
the outside and the bases on the inside. The chains are held together by hydrogen bonds between the
bases on one strand and the bases on the other strand. The distance between 2 strands is relatively
constant, so a purine must pair with pyrimidine. Adenine forms hydrogen bonds (2) with thymine
whereas cytosine forms hydrogen bonds (3) with guanine.

Chargaff's data showing that [adenine] = [thymine] and [guanine] = [cytosine] could be explained if
adenine (A) always paired with thymine (T) and guanine (G) always paired with cystosine (C). This
means the two strands are complementary to each other.
If phosphate attached with 3rd carbon of upper sugar and 5th carbon of lower sugar than direction is
3'–5".
and if phosphate attached with 5th carbon of upper sugar and 3rd carbon of lower sugar than direction
is 5' – 3". Direction of phosphodiester bond in both strand is opposite (antiparallel)

3'
5'

GC
11.1 Å A =T
T =A
S –A=T– S A =T
P 2.8-3.0 Å P
CG
S–GC–S GC
T=A
CG
P 3.4 Å P
S –T =A– S T=A
GC
T=A
P P T=A
S–CG–S
T=A
20 Å T=A
G C
GC

5'

Double strand helix structure for DNA

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 B I O M O LE C U LE S

3'
OH
5' O
C
T A
O
3.4 Å P

P
O
G C
O
P

5' P 3'
O

T A
O
P

P
O

T A
O
P
3' 5'
P
O
G C
O
P

P
O
C G
O
3' 5' C
HO

Complementary base pairing in DNA

[A] = [T]
[G]  [C]

In secondary structure of RNA, helices are present which are only single stranded. Sometimes they fold
back on themselves to form a double helix structure. RNA molecules are of three types and they
perform different functions. They are named as messenger RNA (m-RNA), ribosomal RNA (r-RNA)
and transfer RNA (t-RNA)
DNA Fingerprinting
Every individual has unique fingerprints. These occur at the tips of the fingers and have been used for
identification for a long time but these can be altered by sugery. Asequence of bases on DNA is also
unique for a person and information regarding this is called DNA fingerprinting . It is same for every cell
and cannot be altered by any known treatment. DNA fingerprinting is now used.
(i) in forensic laboratories for identification of criminals.
(ii) to determine paternity of an individual.
(iii) to identify the dead bodies in any accident by comparing the DNA's of parents or children.
(iv) to identifyracial groups to rewrite biological evolution.
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Biological Function of Nucleic acids

Function of RNA and DNA
1. Functions of RNA
(a) There are three types of RNA in the living cell and they perform different roles as given below :

(i) Messenger RNA (m-RNA) carries the message of DNA for performing a particular synthesis.
(ii) Ribosomal RNA (r-RNA) makes provision for a site for performing synthesis of protein.
(iii) Transfer RNA(t-RNA) directs the amino acids to the site for the purpose of synthesis.

(b) Process of leaving and memory stage are believed to be controlled by RNA.

2. Functions of DNA
(a) It has the property of self-replication and is responsible for maintaining hereditary traits from one
generation to the next.

(b) The sequence of DNA gets altered by the action of UV light, X-rays and certain chemical. This
process is called mutation. These mutations are responsible for changing hereditary traits of animal and
their offsprings.

(c) It controls the synthesis of RNA which guides the synthesis of proteins.

The vast differences in heredity among species and among members of the same species are determined
by the sequence of the bases in DNA.

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 B I O M O LE C U LE S
EXERCISE-1 (Subjective Questions)

Q.1 Number of 1° and 2° alcoholic group in sucrose are x and y value of x & y is

Q.2 Number of chiral centre in maltose are ________.

Q.3 Number of Chiral carbons in Fischer projection of D-Fructose in which are OH groups are in RHS are
__________.

Q.4 Number of chiral carbon in Haworth structure of -Glucopyranose having OH group downside are
________.

Q.5 Saccharic acid can be obtained by oxidation of glucose number of C, H and O present in Saccharic acid
are _________.

Q.6 D-Glucose, D-Mannose and D-Fructose form same osazone on reaction with phenyl hydrazine because
they have same confuguration at carbon x,y & z. Values of x, y and z are ____

Q.7 How many different peptides can be synthesised from

(a) Glycine and alanine, and
(b) GlyAla2?

Q.8 Explain how the following reagents denature protein:

(a) Ag+ and Pb2+ (b) Ethanol (c) Urea (d) Heat

Q.9 How are -amino acids, peptides and protein related to each other? How are -amino acids and
dipeptide synthesised?

Q.10 What are peptides? Using a suitable protecting group, sketch the synthesis of a dipeptide.

Q.11 What are proteins? Discuss, with diagram, -pleasted sheet structure of proteins.

Q.12 How will you synthesise glycine from potassium phthalimide?

Q.13 Why are amino acids called amphoteric compounds?

Q.14 What are -amino acids? Given evidence supporting their dipolar ionic structure?

Q.15 Explain the terms :

(a) Denaturation of proteins (b) Isoelectric points

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 B I O M O LE C U LE S
EXERCISE-2 (Objective Questions)
[SINGLE CORRECT CHOICE TYPE]
Q.1 The commonest disaccharide has the molecular formula
(A) C10H18O9 (B) C10H20O10 (C) C18H22O11 (D) C12H22O11
Q.2 On complete hydrolysis of starch, we finally get
(A) Glucose (B) Fructose
(C) Glucose and fructose (D) Sucrose
Q.3 The term anomers of glucose refers to
(A) Isomers of glucose that differ in configurations at carbons one and four (C–1 and C-4)
(B)Amixture of (D)-glucose and (L)-glucose
(C) Enantiomers of glucose
(D) Isomers of glucose that differ in configuration at carbon one (C–1)
Q.4 Which of the following is an example of aldopentose?
(A) Erythrose (B) Ribose (C) Fructose (D) Dihydroxyacetone
Q.5 Glucose and fructose form
(A) Same osazone (B) Same acid on oxidation
(C) Same alcohol when reduced (D) Different osazone
Q.6 The change of optical rotation of glucose solution with time is refered to as:
(A) Mutarotation (B) Inversion (C) Specific rotation (D)Autorotation
Q.7 To become a carbohydrate a compound must contain at least:
(A) 2 carbon atoms (B) 3 carbon atoms (C) 4 carbon atoms (D) 6 carbon atoms
Q.8 Methyl--D-glucoside and methyl--D-glucoside are
(A) Epimers (B)Anomers
(C) Enantiomers (D) Conformational diastereomers
Q.9 Which one of the following is laevorotatory
(A) Glucose (B) Sucrose (C) Fructose (D) None of these
Q.10 Which of the following is a disaccharide
(A) Lactose (B) Starch (C) Cellulose (D) Glucose
Q.11 The two functional groups present in a typical carbohydrate are
(A) – OH and – COOH (B) – CHO and – COOH

(C) > C = O and – OH (D) – OH and  C  O  R

||
Q.12 The monomer of cellulose is O
(A) Fructose (B) Galactose (C) Glucose (D) None of these
Q.13 Glucose is a
(A) Monosaccharide (B) Disaccharide (C) Trisaccharide (D) Polysaccharide
Q.14 Which pair is different for reaction with Fehling solution:
(A) Glucose, Fructose (B) HCHO, CH3CHO
(C) CH2COCH3, C6H5CHO (D) Glucose, Sucrose
Q.15 Glucose contains in addition to aldehyde group
(A) One secondary OH and four primary OH groups
(B) One primary OH and four secondary OH groups
(C) Two primary OH and three secondary OH groups
(D) Three primary OH and two secondary OH groups
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 B I O M O LE C U LE S

Q.16 Glucose reacts with excess of phenyl hydrazine and forms

(A) Glucosazone (B) Glucose phenyl hydrazine
(C) Glucose oxime (D) Sorbitol
Q.17 Hydrolysis of sucrose is called:
(A) Thermal decomposition (B) Saponification
(C) Inversion (D) Hydration
Q.18 Which of the following pentoses will be optically active

CHO CHO CHO

| | |
HCOH HCOH HCOH
| | |
HOCH HCOH HCOH
| | |
HCOH HOCH HCOH
| | |
H 2COH H 2COH H 2COH
I II III

(A)All (B) II and III (C) I (D) II

Q.19 Which of the following statement is incorrect for maltose.
(A) It is a disaccharide (B) It undergoes mutarotation
(C) It is a reducing sugar (D) It does not have hemiacetal group.
Q.20 Naturally occuring (+) - sucrose is :
(A) -D-glucopyronoside--D-fructofuranoside
(B) -D-glucopyronoside--D-fructofuranoside
(C) -D-glucopyronoside--D-fructofuranoside
(D) -D-glucopyronoside--D-fructofuranoside

CHO
H OH
Q.21 H OH D-Ribose when treated with dilute HNO3 forms.
H OH
CH2OH

HO O
HO O
H OH
OH
(A) H ,Achiral (B) HO H , Chiral
H OH
H OH
H OH
O O OH
HO

HO O HO O
H OH H OH
(C) HO H , Achiral (D) H OH , Chiral
H OH H OH
HO O O OH

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
Q.22 Glucose (
i ) HCN / H 3O
   P
(ii ) P / HI

P is :
(A) n- heptanoic acid (B) 2-methyl hexanoic acid
(C) n-heptane (D) 2-methyl hexane

Q.23 Mutarotation involves

(A) Racemisation (B)Diastereomerisation
(C) Optical resolution (D)Conformational inversion

Q.24 Which of the following compounds will not show mutarotation:

(A) -D (+) glucopyranose (B) -D(+) glucopyranose
(C) Methyl--D-glucopyranoside (D) -D(+) galactopyranose

Q.25 Glycogen on hydrolysis gives:

(A) Lactose and Glucose (B) Only Glucose
(C) Glucose and Fructose (D) Glucose and Maltose

Q.26 An example of disaccharide made up of two unit of the same monosaccharide.

(A) Maltose (B) Sucrose (C) lactose (D) None

Q.27 The colour of the precipitate formed when a reducing sugar is heated with Fehling solution is:
(A) Brown (B) Red (C) Blue (D) Green

Q.28 Osazone formation involves only 2 carbon atoms of glucose because of

(A) Oxidation (B) Chelation (C) Reduction (D) Hydrolysis

Q.29 Methyl--D-glucose and methyl --D-glucose are

(A) Epimers (B)Anomers (C) Enantiomers (D) Constitutional isomers

Q.30 Hydrolysis of lactose with dilute acid yield

(A) Equimolar mixture of D-glucose and D-glucose.
(B) Equimolar mixture of D-glucose and D-galactose.
(C) Equimolar mixture of D-glucose and D-fructose.
(D) Equimolar mixture of D-galactose and D-galactose.

Q.31 Glucose does not react with

(A) 2,4-DNP (B) Schiff's reagent (C) NaHSO3 (D)All of these

Q.32 Which statement is incorrect.

(A)All monosaccharide whether aldose or Ketose are reducing sugars
(B) Lactose is present in milk
(C) Fehling solution and Tollen's reagent can reduce, reducing sugars
(D) Glucose is aldohexose

Q.33 In Fructofuranose –OH group of which carbon adds to >C=O group.

(A) C3 (B) C4 (C) C5 (D) C2

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Q.34 Hydrolysis of d-sucrose results in change of optical rotation because

(A) number of moles of d-Glucose are less than number of moles of l-Fructose produced during hydrolysis.
(B)Angle of rotation of l-Fructose is greater thanAOR of d-Glucose
(C) Both glucose and fructose are levorotatory.
(D) Glucose is l and fructose is d and number of moles of glucose formed during reaction are greater
than number of moles of fructose.

Q.35 Which branch of chemistry pursuit of knowledge of what goes on chemically within a living system :
(A) Stereochemistry (B) Biochemistry (C) Both (A) and (B) (D) None

Q.36 Which biomolecules are essential constituents of our food

(A) proteins (B) carbohydrates (C) Both (A) and (B) (D) None

Q.37 What is general formula of carbohydrate

(A) Cx+1(H2O)y (B) Cx(H2O)y (C) Cx(H2O)y+1 (D) Cx+2(H2O)y

Q.38 Carbon hydrate are known by :

(A)Vitamin (B) Carbohydrate (C) Lipid (D) None

Q.39 Carbohydrates is :
(A) Optically inactive polyhydroxy aldheydes or ketones
(B) Optically active polyhydroxy aldheydes or ketones
(C) Both (A) and (B)
(D) None

Q.40 Sugar present in milk is known as

(A) fructose (B) glucose (C) lactose (D) None

Q.41 Carbohydrates are called :

(A) sugar (B) Saccharides (C) Both (A) and (B) (D) None

Q.42 On the basis of hydrolysis carbohydrates are :

(A) Monosaccharides (B) Oligosaccharides (C) Polysaccharides (D)All of these

Q.43 Carbohydrate that cannot be hydrolysed further to give simpler unit of polyhydroxy aldehyde or ketone
is called :
(A) Monosaccharide (B) Poly saccharide (C) Oligo sacharides (D) None

Q.44 Monosaccharides are :

(A) Glucose (B) Fructose (C) Ribose (D)All

Q.45 Carbohydrates that yield two to ten monosaccharic units, on hydrolysis, are called :
(A) Monosaccharides (B) Oligo saccharides (C) Polysacharides (D)All

Q.46 Disaccharides, trisaccharides and tetrasccharides are part of :

(A) Mono saccharides (B) Oligo saccharides
(C) Polysaccharides (D) None

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Q.47 On sucrose hydrolysis we obtain :

(A) 2 molecule glucose (B) 2 molecule fructose
(C) 1 molecule glucose & 1 molecule fructose (D)All

Q.48 On maltose hydrolysis we obtain :

(A) 2 Molecule glucose
(B) 2 molecule fructose
(C) 1 molecule glucose and 1 molecule fructose
(D) None

Q.49 Carbohydrates which yield a large number of monosaccharide units on hydrolysis are called
(A) Monosaccharides (B) Oligosuccharides
(C) Polysaccharide (D)All

Q.50 Choose Polysaccharides

(A) Starch (B) Cellulose
(C) Glycogen and gums (D)All

Q.51 Polysaccharides are

(A) Sugar (B) Non-sugar (C) Both (A) and (B) (D) None

Q.52 Reducing sugars are :

(A) reduce felhing's solution (B) Reduce Tollen's reagent
(C) Both (A) and (B) (D) None

Q.53 Aldose or ketose are :

(A) Non-reducing sugar (B) Reducing sugar
(C) Both (A) and (B) (D) None

Q.54 In sucrose, the reducing groups are bonded then

(A) Sucrose is reducing sugar (B) Sucrose is non reducing sugar
(C) Both (A) and (B) (D) None

Q.55 If Mono saccharide contain aldehyde and keto group then it called respectively :
(A) Ketose, Ketose (B)Aldose,Aldose (C) Aldose, Ketose (D) Ketose, Aldose

Q.56 Fill in the blank respectively :

(i) Triose +Aldehyde group ––––– (ii) Pentose + keto group –––––
(iii) heptose +Aldehyde group
(A) Aldotriose,Aldopentose, Ketoheptose (B) Aldotriose, Ketopentose,Aldoheptose
(C) Ketotriose,Aldopentose, Aldoheptose (D) None

Q.57 Glucose is present in :

(A) Sweet fruits (B) Honey (C) Both (A) and (B) (D) None

Q.58 C12H22O11 HCl

 orH   x + y, where x and y are in equal amount then x and y are respectively
2SO 4

(A) x  Glucose, y  Glucose (B) x  Glucose, y  Fructose

(C) x  Fructose, y  Fructose (D) None

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 B I O M O LE C U LE S

(C6H10O5)n + nH2O 393K ,  x, x is :

dil . H 2SO 4
Q.59 2-3atm

Starch
(A) Fructose (B) Rybose (C) Glucose (D) None
Q.60 Glucose is :
(A) Ketohexose and dextrose (B)Aldohexose and levose
(C)Aldohexose and dextrose (D) None
Q.61 Glucose is Monomer of
(A) Starch (B) Cellulose (C) Both (A) and (B) (D) None

Glucose 
HI
Q.62  x, then x is :
(A) Cyclo pentane (B) n-Hexene (C) n-Hexane (D) Cyclo Hexane

NH2OH
x
Q.63 C6H12O6 , then x and y are respectively ; and here both reaction showthat, in glucose
HCN y
carbonyl group is present.
(A) Hydrin, amine (B) Hydroxylamine, cyanohydrin
(C) Cyanohydrin, hydroxylamine (D) None

C6H12O6 water

Br2
Q.64 x, x is :
(A) Glucose (B) Fructose (C) Gluconic acid (D) None
C HO
O|
||
Q.65 C6H12O6 
 (C H  O  C CH 3 ) 4 , then x is :
x

|
|
O
||
CH 2  O  C CH 3
(A) Br2water (B)AceticAnhydride (C) HI (D) HCN

x Oxidation
 z Oxidation
 y, here z  saccharic acid then x and y are respectively :
HNO3 HNO3
Q.66
(A) Glucose, fructose (B) Glucose, gluconic acid
(C) Sucrose, lactose (D) None
Q.67 Choose correct option
CHO COOH COOH
H OH H OH H OH
HO H HO H HO H
(I) H OH (II) H OH (III) H OH
H OH H OH H OH
CH2OH CH2OH COOH
(a) Gluconic acid (b) Saccharic acid (c) Glucose
(A) I–a, II–b, III–c (B) I–c, II–b, III–a (C) I–c, II–a, III–b (D) I–a, II–c, III–b

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Q.68  and  form of Glucose obtained at particular condition, then condition are respectively :
(A)  from concentrated solution of glucose at 303 K
 from concentrated solution of glucose at 371 K
(B)  from concentrated solution of glucose at 303 K
 from hot and saturated aqueous solution at 371 K
(C) Both (A) and (B)
(D) None
Q.69 -Glucose and –glucose melting point are respectively :
(A) 419 K, 200 (B) 419 K, 423 K (C) 423 K, 419 (D) 500 K, 1000 K
Q.70 In cyclic form of glucose, which carbon –OH involve :
(A) C – 1 (B) C – 3 (C) C – 6 (D) C – 5
Q.71 Two cyclic form of glucose differ only in the configuration of hydroxyl group at Cl, is called and both
form are called :
(A) Mesomeric carbon, mesomer (B)Anomeric carbon, anomer
(C) Both (A) and (B), mesomer and anomer (D) None
Q.72 In pyran :
(A) 2 oxygen and 6 carbon atom (B) 1 oxygen and 5 carbon atom
(C) 1 oxygen and 5 carbon atom (D) 2 oxygen and 4 carbon atom
Q.73 Cyclic structure of glucose is called :
(A) pyranose structure(B) furanose structure (C) sucrose structure (D) fructose structure
Q.74 Fructose is obtained by and it is
(A) Pyran, aldohexose (B) Sucrose, aldohexose
(C) Sucrose, ketohexose (D) Pyran, ketohexose
Q.75 Fructose have ketonic group at
(A) C–1 (B) C–2 (C) C–3 (D) C–5
Q.76 Fructose cyclic forms obtained –OH addition from
(A) C–2 (B) C–3 (C) C–5 (D) C–6
Q.77 Furan have
(A) 1 oxygen atom and 5 C-atom (B) 2 oxygen atom and 4 C-atom
(C) 3 oxygen atom and 3 C-atom (D) 1 oxygen atom and 4C-atom
Q.78 Fructose structure is known as
(A) Pyranose (B) Furanose (C) Rybose (D) None
Q.79 Two mono saccharide units are linked by oxygen atom, this type linkage is called ?
(A) pyranic linkage (B) glycosidic linkage (C) furanic linkage (D) pyrafuranic linkage
Q.80 Sucrose + H2O  x + y, x and y are :
(A) x  D – (+) – Glucose, y  D – (+) – fructose
(B) x  D – (–) – Glucose, y  D – (–) – fructose
(C) x  D – (+) – Glucose, y  D – (–) – fructose
(D) x  D – (+) – Glucose, y  L – (–) – fructose
Q.81 –D–Glucose and -D–fructose linke by glycosidic linkage, by :
(A) C 1 of -glucose, C 2 of -fructose (B) C 2 of -glucose, C 5 of -fructose
(C) C 3 of -glucose, C 3 of -fructose (D) None
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Q.82 Sucrose is dextrorotatory but after hydrolysis it give :

(A) dextrorotatory glucose (B) Levorotatory fructose
(C) Both (A) and (B) (D) None

Q.83 Sucrose Hydrolysis

  solution is net laevorotatory so product name is :
(A) Identical sugar (B) Invert sugar (C) Both (A) and (B) (D) None

Q.84 Maltose is compose of 2 -D-glucose by C1 of one glucose and by –

(A) C3 of other glucose (B) C4 of other glucose
(C) C6 of other glucose (D) C2 of other glucose

Q.85 Choose reducing and non-reducing sugar respectively :

(A) Maltose, sucrose (B) Sucrose, maltose (C) Sucrose, Sucrose (D) None

Q.86 In lactose linkage between the carbon :

(A) C1 of galactose and C3 of glucose (B) C1 of galactose and C2 of glucose
(C) C1 of galactose and C4 of glucose (D) C2 of galactose and C2 of glucose

Q.87 Choose reducing sugar :

(A) Maltose (B) Lactose (C) Glucose (D)All of these

Q.88 Main storage polysaccharide of plants is

(A) Celluslose (B) Starch (C) Glycogen (D) None

Q.89 Starch is polymer of

(A) -Glucose (B) -Glucose (C) Both (A) and (B) (D) None

Q.90 Starch component is :

(A)Amylose (B)Amylopectin (C) Both (A) and (B) (D) None

Q.91 Which component of starch is water soluble :

(A)Amylose (B)Amylopectin (C) Both (A) and (B) (D) None

Q.92 Which component of starch is water insoluble

(A)Amylopectin (B)Amylose (C) Both (A) and (B) (D) None

Q.93 In Amylose, glycosidic bond present in b/w

(A) C1 and C4 (B) C2 and C2 (C) C4 and C5 (D) None

Q.94 Amylose is ______ andAmylopectin is ______ polymer

(A) Branched, unbranched (B) Branched, branched
(C) Unbranched, branched (D) None

Q.95 Amylose and amylopectin contain starch respective

(A) 15–20%, 85–80% (B) 85–80%, 15–20%
(C) 50%, 50% (D) 40% , 60 %

Q.96 InAmylopectin branching occur by :

(A) C1 – C5 linkage (B) C1 – C6 linkag (C) C2 – C4 linkage (D) C3 – C3 linkage
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Q.97 Cellulose is compose of

(A) -D-glucose, -D-glucose (B) -D-glucose, Glucose only
(C) -D-glucose only (D) None

Q.98 In cellulose glycosidic bond is present between

(A) C1 and C4 (B) C5 and C6 (C) C4 and C4 (D) C1 and C1

Q.99 Carbohydrates are stored in animal body as

(A) Cellulose (B) Glycogen (C) Both (A) and (B) (D) None

Q.100
(i) Animal starch is :
(A) Cellulose (B) Glycogen (C) Both (A) and (B) (D) None
(ii) Glycogen is found in :
(A)Animal (B) Yeast (C) Fungi (D)All of these

Q.101 Which compound can exist in a dipolar (zwitter ion) state

(A) C6H5CH2CH(N = CH2) COOH (B) (CH3)2CH·CH(NH2)COOH
(C) C6H5CONHCH2COOH (D) HOOC·CH2CH2COCOOH
COO¯

Q.102 The pH of the solution containing following zwitter ion species is NH3 H

R
(A) 4 (B)6 (C) 8 (D)9

Q.103 Peptide linkage is -

O O O O
(A) –C – O – (B) –C – NH 2 (C) –C – NH– (D) –C – NH–NH 2

Q.104 Test used to identify peptide linkage in protein is:

(A) Biuret (B) Ninhydrin test (C) Molisch test (D) 2,4-DNP test

Q.105 Among the following L-serine is:

COOH COOH

(A) H2N CH2OH (B) HOCH2 H

H NH2

NH2 CH2OH

(C) H COOH (D) H2 N H

CH2OH COOH

Q.106 Glycine is a unique amino acid because it

(A) has no chiral carbon (B) has a sulphur-containing R group
(C) cannot form a peptide bond (D) is an essential amino acid
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Q.107 The isoelectric point of a protein is

(A) the pH at which the protein in molecule has no charges on its surface
(B) the pH at which the protein in solution has an equal number of positive and negative charge
(C) the electric charge under isothermal condition
(D) none of these

Q.108 The -helix is held in a coiled conformation partially because of

(A) optical activity (B) hydrogen bonding (C) resonance (D) delocalisation

Q.109 Complete hydrolysis of protein produces

(A) ammonia and carbon dioxide (B) urea and uric acid
(C) a mixture of amino acids (D) glycogen and a fatty acid

Q.110 The linear arrangement of amino acid units in protein is called

(A) primary structure (B) secondary structure
(C) tertiary structure (D) quaternary structure

Q.111 Source of proteins is/are :

(A) Milk (B) Pulses (C) Fish and Meat (D)All of these

Q.112 "Proteios" mean :

(A) primary importance (B) secondary importance
(C) Tertery importance (D) None

Q.113 Amino acid functional group are :

(A) Only–NH2 (B) Only–COOH
(C) –NH2 and –COOH Both (D) None

Q.114 "Glykos" Mean :

(A) Sweet (B) Salty (C) Tasteless (D) None

Q.115 "tyros" mean :

(A) Sweet (B) Cheese (C) Both (A) and (B) (D) None

Q.116 –NH2 and –COOH, group are present on same carbon then these type acid called :
(A) -amino acid (B) -amino acid (C) –amino acid (D) –amino acid

Q.117 Amino acid, which can be synthesised in the body known as :

(A) Essential aminoacid (B) Non-essential amino acid
(C) Both (A) and (B) (D) None

Q.118 Amino acid, which cannot be synthesised in body known as :

(A) Essential amino acid (B) Non-essential amino acid
(C) Both (A) and (B) (D) None

Q.119 By amino acid, zwitter ion form :

(A) only lose a proton by–COOH group
(B) only accept a proton by –NH2 group
(C) Accept a proton by –NH2 group and lose a proton by –COOH group
(D) None
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Q.120 Zwitter ion react as :

(A)Acid (B) Base (C) Both (A) and (B) (D) None

Q.121 All -aminoacid in protein connected by

(A) Glycosidic bond (B) Peptide bond (C) Both (A) and (B) (D) None

Q.122 Peptide bond form by :

(A) only –COOH group (B) only –NH2 group
(C) –COOH and –NH2 group (D) None

Q.123 When more than 10 amino acid are link by peptide bond then it called :
(A) decapeptides (B) penta-penta-peptides
(C) Poly peptides (D)All of these

Q.124 Insulin have :

(A) 51 amino acid (B) 102 amino acid (C) 110 amino acid (D) 10 amino acid

Q.125 In fibrous proteins, polypeptide chain run parallel together, they held by :
(A) Hydrogen bond (B) disulphide bond (C) Both (A) and (B) (D) None

Q.126 Choose protein which insoluble in water :

(A) Keratin (present in hair) (B) Myosin (present in muscles)
(C) Both (A) and (B) (D) None

Q.127 Choose protein soluble in water :

(A) fibrous (B) Globular (C) Both (A) and (B) (D) None

Q.128 Choose proteins soluble in water :

(A) Insulin (B) albumins (C) Both(A) and (B) (D) None

Q.129 Choose secondary structure proteins :

(A) -Helix (B) -Pleated sheet (C) Both (A) and (B) (D) None

Q.130 In -Helix and -pleated sheet structure, structure is folded by :

(A) Covelent bond b/w  C  and –NH– (B) Ionic bond b/w  C  and –NH–
|| ||
O O
(C) Hydrogen bond b/w  C  and –NH– (D) None
||
O

Q.131 3º and 2º proteins structures are stablised by :

(A) H-bonding (B) disulphide linkage and electrostatic force
(C) Vander waals force (D)All of these

Q.132 Due to above changes globules unfold and helix get uncoiled and proteins loses its biological activity this
is called :
(A) Saturation of protein (B) Naturation of protein
(C) Denaturation of protein (D)All of these

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Q.133 During denaturation of protein which type of structure not affected

(A) 3º (B) 2º (C) 1º (D)All of these

Q.134 In DNA molecule sugar is :

(A) –D–2–de oxyribose (B) -D-ribose
(C) Both (A) and (B) (D) None

Q.135 The particles in nucleus of the cell, responsible for heredity are called :
(A)Vitamin (B) Chromosomes (C) Lipid (D)All of these

Q.136 Nucleic acid are :

(A) DNA (B) RNA (C) Both (A) and (B) (D) None

Q.137 Nucleic acids are long chain polmer of

(A) Nucleosides (B) Nucleotides (C) Both (A) and (B) (D) None

Q.138 DNA (or RNA) yields of :

(A) Pentose sugar
(B) Phosphoric acid
(C) Nitrogen containing heterocyclic compounds
(D)All of these

Q.139 In RNA molecule sugar is :

(A) -D-ribose (B) -D-2-deoxyribose
(C) Both (A) and (B) (D) None

Q.140 Choose correct base for DNA :

(A)Adenine(A), Guanine(G) (B) Cytosine (C)
(C) Thymine (T) (D)All of these

Q.141 Choose correct base for RNA :

(A)Adenine (A), Uracil (U) (B) Cytosine(C)
(C) Guanin(G) (D)All of these

Q.142 A unit formed by the attachment of a base to 1' position of sugar is known :
(A) Nucleotide (B) Nucleoside (C) Both (A) and (B) (D) None

Q.143 Nucleoside is linked to phosphoric acid at

(A) 5'–position of sugar (B) 4'–position of sugar
(C) 6'– position of sugar (D) None

Q.144 Nucleotides are joined together by phosphodiester linkange b/w :

(A) 5' and 4' carbon atoms of pentose sugar (B) 5' and 5' carbon atoms of pentose sugar
(C) 5' and 3' carbon atoms of pentose sugar (D) 5' and 2' carbon atoms of pentose sugar

Q.145 Adenine and cytosine forms H-bond, with respectively :

(A) thymine, guanine (B) Guanine, thymine
(C) thymine, thymine (D) guanine, guanine

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Q.146 Choose correct RNA type :

(A) m-RNA <Messenger RNA> (B) r-RNA <ribosomal RNA>
(C) t-RNA <transfer RNA> (D)All of these

Q.147 DNA fingerprintinguse in

(A) In forensic laboratories
(B) To determine paternity of an individual
(C) To identify racial groups to rewrite biological evolution
(D)All of these

Vitamin & Enzymes

Q.148 Biocatalysts are called :
(A) Protein (B) Lipid (C) Enzymes (D)All of these

Q.149 Almost all the enzymes are :

(A) Globular protein (B) Fibrous protein (C) Both (A) and (B) (D) None

Q.150 Maltose  
x Glucose, then x enzyme is :
(A) Diastase (B) Maltase (C) Pepsin (D) Tripsine

Q.151 Certain organic compuonds are required in small amounts in our diet but their deficiency causes specific
disease these compound are called :
(A) Lipid (B) Protein (C) Vitamins (D)All of these

Q.152 Vitamins which are soluble in fat, but not in water

(A) A (B) D (C) E & K (D)All

Q.153 Choose water soluble vitamin :

(A) B group (B1, B2, B6, B12) (B) Vitamin C
(C) Both (A) and (B) (D) None

Q.154 Which vitamin store in our body :

(A) B1 (B) B2 (C) B6 (D) B12

[MULTIPLE CORRECT CHOICE TYPE]

Q.155 Carbohydrates may be :

(A) Sugars (B) Starch
(C) Polyhydroxy aldehyde/ ketones (D) Compounds that can be hydrolysed to sugar

Q.156 Select the correct statement :

(A) S-glyceraldehyde is also known as L-glyceraldehyde
(B) The configuration of the stereocenter most distant from the carbonyl group determines whether a
monosaccharide is D or L.
(C) Glucose and all naturally occurring sugars are D-sugars
(D) D-erythrose and D-threose are diastereomers.

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Q.157 Select the incorrect statement.

(A) Monosaccharide are insoluble in organic solvents like diethyl ether.
(B) Anomers of a cyclic monosaccharides differ in the position of the OH group at the hemiacetal
carbon.
(C) D-ribose the OH group used to form the five membered furanose ring is located on C4.
(D)Aldopentoses and ketohexoses form pyranose rings in solution.

Q.158 All sixteen possible aldohexose have been isolated or synthesised. Only three occur in nature there are
(A) D-Glucose (B) D-Galatose (C) D-Mannose (D) L-Mannose

Q.159 Which is not correct about monosaccharides.

(A) Optically active polyhydroxy carbonyl compounds.
(B) Fructose & glucose can not be distinguish by Br2/H2O
(C) Glucose and mannose are anomers
(D) Fructose & glucose can be distinguish by Fehling solution

Q.160 Which of the following is diasaccharides ?

(A) Lactose (B) Sucrose (C) Cellulose (D) Maltose

Q.161 Which of the following carbohydrates developes blue colour on treatment with iodine solution ?
(A) Glucose (B)Amylose (C) Starch (D) Fructose

Q.162 Glycosidic linkage is present in :

(A) sucrose (B) starch (C) glucose (D) fractose

Q.163 Free aldehyde group can be produced on hydrolysis of which compound(s) :

(A) maltose (B) sucrose (C) -D Glucose (D) Lactose

Q.164 Which is non reducing sugar :

(A) maltose (B) sucrose (C) Lactose (D)All of these

Q.165 Which statement are correct about following?

6 1
CH2OH CH2OH
O O
5 H
H H H 2 5
4 1 CH2OH
HO OH H O H HO
3 2 3 4
H OH HO H
(A) It is sucrose
(B) Due to presence of heme acetal linkage it is non reducing sugar.
(C) Left side unit is -D-Glucose and rightside unit is -D-fructose.
(D) Due to absence of heme acetal linkage it can't show mutarotation.

Q.166 Select the correct statement.

(A) Proteins upon hydrolysis gives -amino acid only.
(B) Except glycine, all other naturally occuring -amino acids are optically active.
(C) In fibrous proteins polypeptide chains are held together by hydrogen and disulphide bonds.
(D) Fats upon hydrolysis gives -amino acids
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Q.167 Select the correct statement.

(A) Coiling of polypeptide chain form fibrous protein.
(B) Quarternary structure of protein also exist.
(C) Lysine is an amino acid with basic side chain.

(D) The absolute configuration of H 3 N – CH(CH2OH)COO¯ (L-serine) is S.

[REASONING TYPE]

Q.168 Statement 1 : Bromine water changes glucose to gluconic acid.

Statement 2 : Bromine water acts as oxidising agent.
(A) Statement-1 is true, statement-2 is true and statement-2 is correct explanation for statement-1.
(B) Statement-1 is true, statement-2 is true and statement-2 is NOT the correct explanation for statement-1.
(C) Statement-1 is true, statement-2 is false.
(D) Statement-1 is false, statement-2 is true.

[MATCH THE COLUMN]

Q.169 Match the column :

Column I Column II
(A) Sucrose (P) Two acetals
(B) Maltose (Q) No hemiacetal
(C) Lactose (R) 1,4'-glycosidic bond
(D) Cellulose (S) Hydrolysis product is glucose

Q.170 Match the column :

Column I Column II
(Carbohydrate) (Properties)

(A) Starch (P) Mutarotation

(B) Sucrose (Q) Non reducing sugar
(C) Lactose (R) -glycosidic bond
(D) Maltose (S) -glycosidic bond
(T) Reducing sugar
(U) Hemiacetal

Q.171 Column I Column II

(Compound) (Relationship)
(A) -D-Glucose and -D-Glucose (P) Functional group isomer
(B) Glucose and Mannose (Q) Anomer
(C) Glucose and Fructose (R) Epimer
(D) -D-Fructo Furanose and
-D-Fructo Furanose

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Q.172 Column I Column II

(Compound) (Relative configuration)
CHO
HO H
(A) H OH (P) D
CH2OH
COOH
H OH
(B) HO H (Q) L
H OH
H OH
COOH
CHO
H OH
HO H
(C)
H OH
HO H
CH2OH
CH2OH
H OH
H OH
(D) HO H
H OH
CHO

Q.173 Column I Column II

(Carbohydrate) (Type)
(A) Glucose (P) Monosaccharide
(B) Sucrose (Q) Oligosaccharide
(C) Maltose (R) Polysaccharide
(D) Glycogen

Q.174 Column I Column II

(Compounds) (Reagents used to differentiate)
(A) Glucose / Fructose (P) Br2 water
(B) Glucose / Sucrose (Q) Fehling's solution
(C) Fructose / Sucrose (R) Tollen's reagent

Q.175 Column I Column II

(Compound) (Characteristic property)
(A) Amylose (P) Polysaccharide
(B) Cellulose (Q) -Glycosidic linkage
(C) Maltose (R) -Glycosidic linkage
(S) Hydrolysed to glucose

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Q.176 Column I Column II

Side chain Name of amino acid
(A) H (P) Alanine
(B) –CH3 (Q) Valine
(C) (CH3)2CH– (R) Glycine
(D) (CH3)2–CH–CH2 (S) Leucine

Q.177 Column I Column II

Side Chain Name of amino acid
(A) CH 3  CH 2  CH  (P) Aspartic acid
|
CH 3
(B) H2N–(CH2)4– (Q) Lysine
(C) HOOC – CH2–CH2– (R) Glutamic acid
(D) HOOC–CH2– (S) Isoleucine

Q.178 Column I Column II

Side Chain Name of amino acid
(A) HO–CH2 (P) Glutamine
(B) HS–CH2 (Q) Cysteine
(C) PhO–C6H4–CH2 (R) Tyrosine
(D) H 2 N  C CH 2  CH 2 (S) Serine
||
O

Q.179 Column I Column II

Vitamin Source
(A) VitaminA (P) Grams
(B) Thiamine (Vitamin B1) (Q) Fish liver oil
(C) Riboflavin (Vitamin B2) (R) Green vegetables
(D) Pyridoxine (Vitamin B6) (S) egg white

Q.180 Column I Column II

Vitamin Source
(A) Vitamin B12 (P) Citrus fruit
(B) Vitamin C (Q) Sunflower oil
(ascorbic acid)
(C) VitaminD (R) Sunlight
(D) VitaminE (S) Meat
(E) Vitamin K (T) Green leaf vegetables

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Q.181 Column I Column II

Vitamin Deficiency diseases
(A) VitaminA (P) Convulsions
(B) Vitamin B1 (Q) PerniciousAnaemia
(thiamine)
(C) Vitamin B2 (R) Beri-Beri
(Riboflavin) (S) Xerophthalmia
(D) Vitamin B6 (T) Cheilosis
(Pyridoxine)
(E) Vitamin B12

Q.182 Column I Column II

Vitamin Deficiency diseases
(A) Vitamin C (P) Increased blood clotting
(B) VitaminD (Q) Rickets
(C) VitaminE (R) Scurvy
(D) Vitamin K (S) Muscular weakness

Q.183 Column I Column II

(A) Invertase (P) Decomposition of urea into NH3 and CO2
(B) Maltose (Q) Conversion of glucose into ethyl alcohol
(C) Pepsin (R) Hydrolysis of maltose in glucose
(D) Urease (S) Hydrolysis of cane sugar
(E) Zymase (T) Hydrolysis of proteins into peptides

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EXERCISE-3
SECTION-A
(JEE ADVANCED Previous Year's Questions)
Q.1 Give the structures of the products in each of the following reactions. [JEE 2000]

Sucrose H A + B

Q.2 Aspartame, an artificial sweetener, is a peptide and has the following structure: [JEE 2001]
CH 2  C 6 H 5
|
H 2 N  CH  CONH  CH  COOCH 3
|
CH 2  COOH
(i) Identify the four functional groups.
(ii) Write the zwitterionic structure.
(iii) Write the structures of the amino acids obtained from the hydrolysis of aspartame.
(iv) Which of the two amino acids is more hydrophobic?

Q.3 Following two amino acids lysine and glutamine form dipeptide linkage. What are two possible dipeptides?
NH2 NH2

H2N COOH + HOOC COOH [JEE 2003]

Q.4 The structure of D-Glucose is as follows- [JEE 2004]

CHO (a) Draw the structure of L -Glucose
H OH (b) Give the reaction of L- Glucose with Tollen's reagent.
HO H
H OH
H OH

HO

Q.5 Which of the following pairs give positive Tollen’s test? [JEE 2004]
(A) Glucose, sucrose (B) Glucose, fructose
(C) Hexanal,Acetophenone (D) Fructose, sucrose

Q.6 Two forms of D – glucopyranose, are called. [JEE 2005]

(A) Enantiomers (B)Anomers (C) Epimers (D) Diastereomers

Q.7 When benzene sulphonic acid and p-nitrophenol are treated with NaHCO3, the gases released
respectively are [JEE 2006]
(A) SO2, NO2 (B) SO2, NO (C) SO2, CO2 (D) CO2, CO2

Q.8 Statement-1 : Glucose gives a reddish-brown precipitate with Fehling’s solution.

because [JEE 2007]
Statement-2 : Reaction of glucose with Fehling’s solution gives Cu2O and gluconic acid.
(A) Statement-1 is True, Statement-2 is True; Statement-2 is a correct explanation for Statement-1.
(B) Statement-1 is True, Statement-2 is True; Statement-2 is NOT a correct explanation for Statement-1.
(C) Statement-1 is True, Statement-2 is False.
(D) Statement-1 is False, Statement-2 is True.

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Q.9 Statement-1 : p-Hydroxybenzoic acid has a lower boiling point than o-hydroxybenzoic acid.
because [JEE 2007]
Statement-2 : o-Hydroxybenzoic acid has intramolecular hydrogen bonding.
(A) Statement-1 is True, Statement-2 is True; Statement-2 is a correct explanation for Statement-1.
(B) Statement-1 is True, Statement-2 is True; Statement-2 is NOT a correct explanation for Statement-1.
(C) Statement-1 is True, Statement-2 is False.
(D) Statement-1 is False, Statement-2 is True.

Q.10 Match the chemical substances in Column I with type of polymers / type of bonds in Column II. Indicate
your answer by darkening the appropriate bubbles of the 4 × 4 matrix given in the ORS. [JEE 2007]
Column I Column II
(A) Cellulose (P) Natural polymer
(B) Nylon-6, 6 (Q) Synthetic polymer
(C) Protein (R) amide linkage
(D) Sucrose (S) Glycoside linkage

Q.11 Cellulose upon acetylation with excess acetic anhydride / H2SO4 (catalytic) gives cellulose triacetate
whose structure is AcO [JEE 2008]
H O O–
AcO H
OAc H
H O O H
AcO H
OAc H H OAc
O O
H H H
(A) OAc H H OAc
–O H AcO
H OAc O O–
H
AcO H
OH H
H O O H
AcO H
OH H H OH
O O
H H H
OH H H OH
(B) – O H
H OH

AcO AcO AcO

H H O H H O H H
H O O–
OAc H H
OAc H OAc H
–O O O H
(C) H OAc H OAc H OAc
AcO AcO AcO
O H H O H
H H H O O–
H H
H H H H
–O O H H
O H
(D) OAc OAc OAc OAc OAc OAc
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Q.12 The correct statement(s) about the following sugars X and Y is(are) [JEE 2009]
CH2OH
CH2OH O
CH2OH H H
O H
H H HOH2C O H O H HO
H H O OH
OH H O H
HO H HO CH2OH OH H OH H
HO H
H OH OH H
H OH

(X)
(Y)
(A) X is a reducing sugar and Y is a non-reducing sugar
(B) X is a non-reducing sugar and Y is a reducing sugar
(C) The glucosidic linkages in X and Y are  and  , respectively.
(D) The glucosidic linkages in X and Y are  and  , respectively.

Q.13 Among cellulose, polyvinyl chloride, nylon and natural rubber, the polymer in which the intermolecular
force of attraction is weakest in [JEE 2009]
(A) Nylon (B) Polyvinyl chloride
(C) Cellulose (D) Natural Rubber

Q.14 The correct statement about the following disaccharide is [JEE 2010]
CH2OH
O H CH2OH O
H H
H
OH H H HO
OH CH2OH
OCH2CH2O
H OH OH H
(a) (b)
(A) Ring (a) is pyranose with -glycosidic link.
(B) Ring (a) is furanose with -glycosidic link
(C) Ring (b) is furanose with -glycosidic link
(D) Ring (b) is pyranose with -glycosidic link

Q.15 The following carbohydrate is [JEE 2011]

(A) a ketohexose (B) an aldohexose (C) an -furanose (D) an -pyranose

Q.16 A decapeptide (Mol. Wt. 796) on complete hydrolysis gives glycine (Mol. Wt. 75), alanine and
phenylalanine. Glycine contributes 47.0 % to the total weight of the hydrolysed products. The number
of glycine units present in the decapeptide is [JEE 2011]

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Q.17 The substituents R1 and R2 for nine peptides are listed in the table given below. How many of these
peptides are positively charged at pH = 7.0 ? [JEE 2012]

 
H 3 N  C H  CO  NH  C H  CO  NH  C H  CO  NH  C H  CO O
| | | |
H R1 R2 H

Peptide R1 R2
I H H
II H CH 3
III CH 2COOH H
IV CH 2CONH 2 (CH 2 ) 4 NH 2
V CH 2CONH 2 CH 2CONH 2
VI (CH 2 ) 4 NH 2 (CH 2 ) 4 NH 2
VII CH 2COOH CH 2CONH 2
VIII CH 2OH (CH 2 ) 4 NH 2
IX (CH 2 ) 4 NH 2 CH 3

Q.18 When the following aldohexose exists in its D-configuration, the total number of stereoisomers in its
pyranose form is [JEE 2012]
CHO
|
CH 2
|
CHOH
|
CHOH
|
CHOH
|
CH 2OH

Q.19 Atetrapeptide has –COOH group on alanine. This produces glycine (Gly), Valine (Val), PhenylAlanine
(Phe) andAlanine (Ala), on complete hydrolysis. For this tetrapeptide, the number of possible sequences
(primary structures) with –NH2 group attached to a chiral center is [JEEAdvance 2013]

Q.20 The total number of distinct naturally occuring amino acids obtained by complete acidic hydrolysis
of the peptide shown below is [JEEAdvance 2014]
O
O O H O H O H
N
N N N
N N N

H
N CH2 O H O H CH2 O
O

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Q.21 The structure of D- (+) glucose is : [JEEAdvance 2015]

CHO

H OH

HO H

H OH

H OH

CH 2 OH

The structure of L-(–) glucose is :

CHO CHO CHO CHO

HO H H OH HO H HO H
H OH HO H HO H HO H
HO H H OH H OH HO H
(A) HO (B) HO (C) HO (D)
H H H H OH

CH 2 OH CH 2 OH CH 2 OH CH 2 OH

Q.22 For 'invert sugar', the correct statement(s) is (are) [JEEAdvance 2016]
[Given : specific rotations of (+)-sucrose, (+)-maltose, L-(–)-glucose and L-(+)-fructose in aqueous
solution are +66°, +140°, –52° and +92°, respectively]
(A)'invert sugar' is prepared by acid catalysed hydrolysis of maltose
(B) 'invert sugar' is an equimolar mixture of D-(+)-glucose and D-(–)-fructose
(C) specific rotation of 'invert sugar' is –20°
(D) on reaction with Br2 water, 'invert sugar' forms saccharic acid as one of the products

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Q.23 The Fischer presentation of D-glucose is given below. [JEEAdvance 2018]

CHO
H OH

HO H

H OH

H OH
CH2OH
D-glucose
The correct structure(s) of -L-glucopyranose is (are)

H H
O O
HO CH2 OH OH HO CH2 OH OH

(A) H H HO H (B) H H H H

OH H OH OH

CH2OH H
O O
H H OH HO CH2OH H

(C) HO OH HO H (D) H H HO OH

H H OH H

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SECTION-B
(JEE Main Previous Year's Questions)
Q.1 RNA contains - [AIEEE-2002]
(A) Urasil, Ribose (B) Thiamine, Ribose
(C) Cytocine, Deoxyribose (D)Adenine, Deoxyribose
Q.2 Complete hydrolysis of cellulose gives – [AIEEE-2003]
(A) D-glucose (B) L-glucose (C) D-fructose (D) D-ribose
Q.3 The reason for double helical structure of DNA is operation of – [AIEEE-2003]
(A) Hydrogen bonding (B) Electrostatic attractions
(C) vander Waal’s forces (D) Dipole-dipole interaction
Q.4 Coordination compounds havegreat importancein biological systems, Inthis context whichofthe following
statements is incorrect ? [AIEEE-2004]
(A) Chlorophylls are green pigments in plants and contain calcium
(B) haemoglobin is the red pigment of blood and contains iron
(C) Cyanocobalamin is B12 and contains cobalt
(D) Carboxypeptidase–A is an enzyme and contains zinc
Q.5 Which base is present in RNA but not in DNA ? [AIEEE-2004]
(A) Uracil (B) Cytosine (C) Guanine (D) Thymine
Q.6 Insulin production and its action in human body are responsible for the level of diabetes. This compound
belongs to which of the following categories ? [AIEEE-2004]
(A)Aco-enzyme (B)Ahormone (C)An enzyme (D)An antibiotic
Q.7 Identify the correct statement regarding enzymes : [AIEEE-2004]
(A) Enzymes are specific biological catalysts that can normally function at very high temperatures
(T~ 1000 K)
(B) Enzymes are normally heterogeneous catalysts that are very specific in their action
(C) Enzymes are specific biological catalysts that cannot be poisoned
(D) Enzymes are specific biological catalysts that possess well-defined active sites
Q.8 In both DNA and RNA, heterocylic base and phosphate ester linkages are at – [AIEEE-2005]
(A) C2' and C5' respectively of the sugar molecule
(B) C5' and C2' respectively of the sugar molecule
(C) C5' and C1' respectively of the sugar molecule
(D) C1' and C5' respectively of the sugar molecule
Q.9 The pyrimidine bases present in DNA are – [AIEEE 2006]
(A) cytosine and guanine (B) cytosine and thymine
(C) cytosine and uracil (D) cytosine and adenine
Q.10 The term anomers of glucose refers to – [AIEEE 2006]
(A) a mixture of (D)-glucose and (L)-glucose
(B) enantiomers of glucose
(C) isomers of glucose that differ in configuration at carbon one (C-1)
(D) isomers of glucose that differ in configurations at carbons one and four (C-1 and C-4)

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Q.11 The secondary structure of a protein refers to – [AIEEE 2007]

(A) -helical backbone (B) hydrophobic interactions
(C) sequence of -amino acids (D) fixed configuration of the polypeptide backbone

Q.12 -D-(+)-glucose and -D-(+)-glucose are [AIEEE 2008]

(A) epimers (B) anomers (C) enantiomers (D) conformers

Q.13 The two functional groups present in a typical carbohydrate are : [AIEEE 2009]
(A) – OH and –COOH (B) – CHO and –COOH
(C) > C = O and –OH (D) – OH and –CHO

Q.14 Which of the following compounds can be detected by Molisch's test ? [AIEEE 2012]
(A)Amines (B) Primary alcohols (C) Nitro compounds (D) Sugars

Q.15 Which one of the following statement is correct? [AIEEE 2012]

(A)All amino acids except glycine are optically active.
(B)All amino acids except glutamic acid are optically active.
(C)All amino acids except lysine are optically active.
(D)All amino acids are optically active.

Q.16 Synthesis of each molecule of glucose in photosynthesis involves: [JEE Main 2013]
(A) 10 molecules ofATP (B) 8 molecules ofATP
(C) 6 molecules ofATP (D) 18 molecules ofATP

Q.17 Which one of the following bases is not present in DNA? [JEE Main 2014]
(A)Adenine (B) Cytosine (C) Thymine (D) Quinoline

Q.18 Thiol group is present in : [JEE Main 2016]

(A) Methionine (B) Cytosine (C) Cystine (D) Cysteine

Q.19 Which of the following compounds will behave as a reducing sugar in an aqueous KOH solution ?
[JEE Main 2017]

HOH2C O CH2OH HOH2C O CH2OH

HO HO
(A) (B) OCH3
OH OH

HOH2C
HOH2C O CH2OH
O CH2OCH3
OH HO
(C) (D) OCOCH3
OH
OH OH

Q.20 Glucose on prolonged heating with HI gives: [JEE Main 2018]

(A) Hexanoic acid (B) 6-iodohexanal (C) n-Hexane (D) 1-Hexene

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EXERCISE-4

SECTION-A
(CBSE Previous Year's Questions)
Q.1 What are hormones ? State the function of the following hormones : [CBSE-2003, 3]
(i) Testosterone
(ii) Oxytocin

Q.2 How does DNA replicate ? Describe the mechanism of replication. How is the process responsible for
preservation of heredity ? [CBSE-2004, 5]

Q.3 Write the major classes in which the carbohydrates are divided depending upon whether these undergo
hydrolysis, and if so, on the number of products formed. [CBSE-2004, 2]

Q.4 (a) Write chemical equations for the reactions of glucose with [CBSE-2005, 2]
(i)Acetic anhydride and
(ii)Ammoniacal silver nitrate solution.
(b) What do you understand by replication by DNA ? How does DNA differ from RNA structurally ?
Q.5 (a) Define vitamins and state their classification. List two vitamins of each class. [CBSE-2005, 5]
(b) What are enzymes ? State the activity of an enzyme
Q.6 (a) Write the chemical reactions of glucose with (i) NH2OH and (ii) (CH3CO)2O. Also draw simple
Fischer projections of D-glucose and L-glucose.
(b) Name the food sources and the deficiency diseases caused due to lack of any two of vitamin A, C,
E and K. [CBSE-2005, 5]

Q.7 Describe briefly two important functions of nucleic acid. [CBSE-2005, 3]

Q.8 Can a copolymer be formed in both addition and condensation polymerisation ? Explain with examples.
[CBSE-2005, 2]

Q.9 What are nucleotides ? Name two classes of nitrogen containing bases found in nucleotides.
[CBSE-2005, 2]

Q.10 Describe how allergic response is produced in the body. Write the role of an antihistamine.
[CBSE-2005, 3]

Q.11 (a) What is digestion ? How does digestion of carbohydrate take place ? [CBSE-2005, 3]
(b) Differentiate between DNA and RNA. Give four differences.

Q.12 (a) What are essential and non-essential amino acids ? Give two examples of each.
(b) What are the two types of photosynthesis in green plants ? Give the basic equations of photosynthesis.
(c) Mention the two products of glycolysis. [CBSE-2006, 2]

Q.13 Give one example each for reducing and non-reducing sugars. [CBSE-2006, 1]

Q.14 (i) What changes occur during digestion of a protein in human body ?
(ii) Name the different types of RNA found in the cell. Mention their function [CBSE-2006, 2]

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Q.15 Name the purines present in DNA. [CBSE-2007, 1]

Q.16 (a) What are natural and synthetic polymers ?

(b) Define and classify vitamins. [CBSE-2007, 2]

Q.17 (a) Name the three major classes of carbohydrates and give an example of each of these classes.
(b)Answer the following :
(i) What type of linkage is responsible for the primary structure of propeins ?
(ii) Name the location where protein synthesis occurs in our body. [CBSE-2007, 5]

Q.18 Why do amines react as nucleophiles ? [CBSE-2007, 1]

Q.19 B-complex is an often prescribed vitamins. What is complex about it and what is its usefulness.
[CBSE-2007, 1]

Q.20 (a)Answer the following questions briefly :

(i) What are reducing sugars ?
(ii) What is meant by denaturation of a protein ?
(iii) How is oxygen replenished in out atmosphere ? [CBSE-2007, 3, 2]
(b) Define enzymes :

Q.21 Define the following terms in relation to proteins. [CBSE-2008, 1]

Peptide linkage

Q.22 Write two main functions of carbohydrate in plants. [CBSE-2008, 1]

Q.23 What happens when D-glucose is treated with the following reagents : [CBSE-2008, 3]
(i) HI (ii) Bromine water (iii) HNO3

Q.24 How are the vitamins classified ? Mention the chief sources of vitamins Aand C. [CBSE-2008, 2]

Q.25 Discuss the two ways in which drugs prevent attachment of natural substrate on active site of an enzyme.
[CBSE-2008, 2]

Q.26 What are amino acids ? On electrolysis in an acidic solution, the relevant amino ions migrate towards
the cathode while in alkaline solution they migrate towards the anode. Give reason.
[CBSE-2008, 3]

Q.27 What are essential and non-essential acids ? Give one example of each type. [CBSE-2008, 1]

Q.28 Mention the type of linkage responsible for the formation of the following : [CBSE-2008, 2]
(i) Primary structure of proteins
(ii) Cross-linking of polypeptide chains
(iii) -helix formation
(iv) -sheet structure

Q.29 Name two water soluble vitamin, their sources and the diseases caused due to their deficiency in diet.
[CBSE-2009, 2]

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Q.30 (a) What is the structural difference between a nucleoside and a nucleotide ? [CBSE-2009, 3]
(b) The two strands in DNA are not identical but are complementary.
Explain.

Q.31 What is the biological effect of denaturation of proteins ? [CBSE-2009, 1]

Q.32 Explain the following terms with one example in each case : [CBSE-2010, 3]
(i) Food preservation (ii)Enzymes (iii) Detergents

Q.33 Differentiate between fibrous proteins and globular proteins. What is meant by the denaturation of a
protein ? [CBSE-2010, 3]

Q.34 (a) What type of bonding helps in stabilising the -helix structure of proteins.
(b) Differentiate between globular and fibrous proteins. [CBSE-2010, 3]

Q.35 What are vitamin ? Deficiency of which vitamin causes [CBSE-2010, 2]

(i) Pernicious anaemia (ii) Convulsions

Q.36 What is essentially the difference between -form of glucose and -form of glucose ? Explain.
[CBSE-2011]

Q.37 Explain what is meant by (i) a peptide linkage, (ii) a glycosidic linkage. [CBSE-2011]

Q.38 Name the bases present in RNA. Which one of these is not present in DNA ? [CBSE-2011]

Q.39 Write the main structural difference between DNA and RNAof the four bases, name those which are
common to both DNA and RNA. [CBSE-2011, 2]

Q.40 What are the products of hydrolysis of lactose? [CBSE 2013]

Q.41 What are the products of hydrolysis of maltose? [CBSE 2014]

Q.42 Define the following terms : [CBSE 2014]

(i) Glycosidic linkage
(ii) Invert sugar
(iii) Oligosaccharides

Q.43 (i) Which one of the following is a disaccharide: [CBSE 2015]

Starch, maltose, fructose, glucose
(ii) What is the difference between acidic amino acid and basic amino acid?
(iii) Write the name of the linkage joining two nucleotides.

Q.44 (i) Write one reaction of D-Glucose which cannot be explained by its open chain structure.
(ii) What type of linkage is present in Nucleic acids?
(iii) Give one example each for water soluble vitamins and fat soluble vitamins? [CBSE 2016]

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EXERCISE-5 (Rank Booster)

[SINGLE CORRECT CHOICE TYPE]

Q.1 The correct name of 'sucrose' is
(A) -D-glucopyranosyl--D-fructofuranoside
(B) -D-glucopyranosyl--D-fructofuranoside
(C) -D-glucopyranosyl--D-fructofuranoside
(D) -D-glucopyranosyl--D-fructofuranoside

Q.2 Which set of terms correctly identifies the carbohydrate shown

H O OH
OH H
HOH 2C H
H OH
1. Pentose 2. Hexose
3. Aldose 4. Ketose
5. Pyranose 6. Furanose
(A) 1, 3 and 6 (B) 1, 3 and 5 (C) 1, 4 and 6 (D) 2, 3 and 6
(E) 1,4 and 6

Q.3 Identify the correct statement about lactose.

(A) It consists of one galactose and one glucose unit
(B) Mutarotation is not possible
(C) It is non reducing carbohydrate
(D) Lactase is not used to cleave the –1, 4'-glycoside bond.

Q.4 Consider the given process.

CHO CHOH CHO
H–C–OH C–OH HO–C–H
HO H OH¯ HO H OH¯ HO H
H OH H2O H2O
H OH H OH
H OH H OH H OH
CH2OH CH2OH CH2OH
(I) (II) (III)
and identifythe incorrect statement.
(A) Configuration at C–2 is lost on enolisation
(B) I and III are epimers
(C) Proton transfer from water to C–1 converts ene diol to an aldose.
(D) D-glucose can isomerise to D-fructose through enol intermediate.

Q.5 The configuration of the C-2 epimer of D-glucose is-

(A) 2R, 3S, 4R, 5S (B)2S, 3S, 4R, 5R
(C) 2S, 3R, 4S, 5R (D)2R, 3S, 4R, 5R

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Q.6 Same osazone derivative is obtained in case of D-glucose, D-Mannose and D-Fructose due to
(A) the same configuration at C-5
(B) the same constitution.
(C) the same constitution at C-1 and C-2
(D) The same constitution and same configuration at C-3, C-4, C-5 and C-6 but different constitution
and configuration at C-1 and C-2 which becomes identical by osazone formation.
Q.7 Amylose and cellulose both are linear polymers of glucose. The difference between them is:
(A) Amylose has  (1  4') linkage and cellulose has  (1  4') linkage
(B) Amylose has  (1  4') linkage and cellulose has  (1  4') linkage
(C) Amylose has  (1  4') linkage and cellulose has  (1  6') linkage
(D) Amylose has  (1  4') linkage and cellulose has  (1  6') linkage
Q.8 Celluose is a straight chain polysaccharide composed of
(A) D-glucose units joined by -glycosidic linkage
(B) D-glucose units joined by -glycosidic linkage
(C) D-galactose units joined by -glycosidic linkage
(D) D-galactose units joined by -glycosidic linkage

Q.9 A tripeptide is written as Glycine-Alanine-Glycine. The correct structure of the tripeptide is

O CH3
NH
(A) NH2 NH COOH
O CH3

CH3 O CH3
NH
(B) NH2 NH COOH
O
O
NH
(C) NH2 NH COOH
O CH3

CH3 O
NH
(D) NH2 NH COOH
O CH3
Q.10 Which one of the following structures represents the peptide chain:
H O H O H O
(A) –N–C–C–C–N–C–C–N–C–C–C– (B) –N–C–N–C–NH–C–NH–
H O H
H H H H
(C) –N–C–C–C–C–NH–C–C–C (D) –N–C–C–N–C–C–N–C–C–
O O O

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[PARAGRAPH TYPE]
Paragraph for question nos. 11 to 13
Consider the following reversible process for a reaction of D-glucose.
+
H
Y
CH 2OH O -D-isomer
HO H  CH 3OH
OH  [X]
OH
HO
D-glucose Z
( or  form) + -D-isomer
H
Q.11 The structure of intermediate [X] is
 CH2OH O
CH2OH O
HO OH
(A) (B) OH
OH
HO O
CH 2OH O CH 2OH O
HO HO
(C) (D) OH
O OH
HO HO

Q.12 Select the correct option.

CH2OH O CH 2OH O
HO HO
(A) Y is H (B) Z is OCH 3
OH OH
HO OMe HO H
CH2OH O
CH 2OH O HO
H
(C) Y is OH (D) Z is OH
OH HO OCH3
H
OCH 3

Q.13 Which of the following is positional isomer of -D glucose?

CH2OH O
CH2OH O
HO
(A) OH (B) HO OCH3
HO OH
OCH3 HO

OH OH
CH2OH CH2OH

(C) HO OH (D) HO OCH3

OH OH
O O

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[MULTIPLE CORRECT CHOICE TYPE]

Q.14 Which of the following are correct.
(A) Br2/H2O can be used to differentiate between aldose & ketose.
(B)All monosaccharides are reducing sugar
(C) Osazone formation destroys the configuration about C2 of an aldose but not effect the rest of
molecule
(D) Mono saccharides undergoes mutarotation.

Q.15 -D-(+) Glucopyranose is

(A) Cylic structure of glucose
(B) It is dextrorotatory because 'D' is placed before name of it
(C) it is anomer of -D-(+) Glucopyranose
(D) Pyranose naming is due to it's anlogy with pyrane

Q.16 Which statement(s) is / are correct.

(A) Glucose react with NH2–OH to form oxime.
(B) Pentaacetate of glucose does not react with NH2–OH
(C) HI can reduce glucose to n-Hexane
(D) Glucose reacts with HCN to form epimeric cyonohydrin.

Q.17 Which statement is correct regarding to following structure :

CH2OH CH2OH
HO O H O OH
H O H
OH H OH H
H H
H OH H OH
(A) It is lactose
(B) It is composed of -D-galactose and -D-glucose
(C) Left side unit is galactose and right side unit is glucose
(D) there is free anomeric OH

Q.18 Select the correct option.

(A) Isoelectric point is the pH at which an amino acid exists primarily in its neutral form.
(B) Isoelectric point is the average of pKa values of -COOH amino - NH 3 groups [valid only for
neutral amino acid]
(C) Glycine is characterised by two pKa values.
(D) For neutral amino acid the concentration of zwitter ion is maximum at its isoelectric point.

Q.19 Amino acids are synthesised from.

(A) -Halo acids by reaction with NH3.
(B)Aldehydes by reaction with NH3 and cyanide ion followed by hydrolysis.
(C)Alkyl halides byreaction with the enolate anion derived from diethyl acetamidomalonate & hydrolysis.
(D) Alcohols by reaction with NH3 and CN¯ ion followed by hydroysis.

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[MATRIX TYPE]
Q.20 Match the column :
Column I Column II
CH2OH O
HO H
CH2OH O
(A) HO OH O OH (P) -glycoside bonds
OH
HO H
H OH
O H
CH 2 O OH
HO
(B) OH O (Q) Reducing sugar
OH OH
HO HOCH2

CH 2OH O H
HO
HO
HO
O
HOCH 2 O
(C) (R) Forms enediol intermediate
HO
CH2OH
OH
HOCH2 HOCH2
O O
(D) HO O OH (S) -glycoside bond
HO OH HO OH

Q.21 Column I Column II

(Monosaccharide units on hydrolysis)
(A) Sucrose (P) -D Glucose
(B) Maltose (Q) -D-Fructose
(C) Lactose (R) -D-Glucose
(S) -D-Galactose

Q.22 Column I Column II

(Reactant) (Number of functional group in product)
HI
(A) Glucose  (P) 2
(B) Glucose Br water
2   (Q) 3
(C) Glucose HCN
 (R) 0
O O
CH3–C–O–C–CH3
(D) Glucose (excess)

(E) Glucose HNO

3 

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Q.23 Column I Column II

CH2OH
H O H
H
(A) OH H (P) -D(+)-Glucopyranose
HO OH
H OH
CH2OH
H O OH
H
(B) OH H (Q) -D(+)-Glucopyranose
HO H
H OH
HOH2C O CH2OH

H HO
(C) H OH (R) -D(–)-Fructofuranose
OH H
HOH2C O OH

H HO
(D) H CH2OH (S) -D(–)-Fructofuranose
OH H

[SUBJECTIVE]

Q.24 The pKa values for the three acidic group P,Q,R are 4.3, 9.7 and 2.2 respectively
(R) (P)
HOOC–CH –CH 2–COOH
+
NH3
(Q)
Calculate the isoelectric point of the amino acid ?

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ANSWER KEY
EXERCISE-1

Q.1 3&5 Q.2 10 Q.3 2 Q.4 3 Q.5 6108 Q.6 345

Q.7 (a) Four products can be obtained :

(i) [Link] (ii)[Link] (iii)[Link] (iv) [Link]
(b) These products are possible :
(i) [Link] (ii)[Link] (iii)[Link]

Q.8 (a) Heavy metal cations Ag+ and Pb2+ form insoluble salts with the –COO¯ group.
(b) Ethanol interferes with the hydrogen bonding by offering its own competing hydrogens.
(c) Urea can form a good hydrogen bond and thus interferes with the orignal hydrogen bonding in
the protein.
(d) Heat produces more random conformations in the protein and thus hampers the formation of
helix. Due to these reasons, the denaturation of protein takes place.

Q.9 Protein : The name protein is taken from the Greek word "proteios", which means "first". Of all
chemical compounds, proteins must almost certainly be ranked first, for they are the substance of life.
Proteins make up a large part of the animal body, they hold it together and they run it. They are found in
all living cells. Chemically, proteins are high polymers. They are polyamides and the monomers from
which they arederived are the  - amino carboxylic [Link] protein molecule contains hundreds
or even thousands of amino acid units. These units can be of twenty-odd different kinds. The number of
different combinations, i.e., the number of different protein molecules that are possible, is almost infinite.

Q.10 Peptides are amides formed by interaction between amino groups and carbonyl groups of amino acids.

The amino bonds   NH  C   that link amino acid residues are called peptide bonds. So peptide
 || 
 O 
 

bonds are the only covalent bonds that hold amino acid residues together in a peptide or protein.
Depending upon the number of amino acid residues per molecule, theyare known as dipeptides, tripeptides
and so on and finally polypeptides. (By convention, peptides of molecular weight upto 1000 are known
as polypeptides and above that as protein)

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O O O
  
H3N–CH2–C–NH–CH 2COO  H3N–CH2–C–NH–CH–C–NH–CH–COO
(Gly-Gly) CH3 CH2–Ph
Glycine-Alaninedipeptide (Gly-Ala-Phen Tripeptide)
Glycine-Alanine-phenylalanine

O O

H3N–CH–C–NH–CH–C—NH–CH–COO 
R R R
n
Polypeptide

Dipeptides are made from two amino acids where as oligopeptides are made from 3 to 10 amino acids.
If 11 to 100 amino acids are present together they called polypeptide and 100 onwards they are called
as macropeptide.
O O O O

H2N–CH2–C–OH + H2N–CH2–C–OH – NH–CH 2–C–NH–CH2–C –

n
+ peptide linkage
PhCOCl ROH/H
O O O O O

Ph–C–NH–CH2–C–OH H2N–CH2–C–OR Ph–O–C–NH–CH2–C–NH–CH2–C–OR
For the synthesis of polypeptides, the amino groups that are not to be linked in peptide bonds must be
blocked so as to be unreactive. Then all other reactive functional groups must be protected to prevent
their participation in the coupling produces. The coupling must be effected by a method that does not
cause racemization or chemical alternation of the side chains.

Q.11 You have already read that proteins are the polymers of -amino acids and they are connected to each
other by peptide bond or peptide linkage. Chemically, peptide linkage is an amide formed between —
COOH group and — NH2 group. The reaction between two molecules of similar or different amino
acids, proceeds through the combination of the amino group of one molecule with the carboxy1 group of
the other. This results in the elimination of a water molecule and formation of a peptide bond — CO —
NH —. The product of the reaction is called a dipeptide because it is made up of two amino acids. For
example, when carboxy1 group of glycine combines with the amino group of alanine we get a dipeptide,
glycylalanine.

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H2N — CH2 — COOH + H2N — CH — COOH

– H2O CH3

H2N — CH2 — CO — NH — CH — COOH

CH3
Peptide linkage

Glycylalanine (Gly-Ala)

In -structure all peptide chains are stretched out to nearlymaximum extension and then laid side by side
which are held together, by intermolecular hydrogen bonds. The structure resembles the pleated folds of
drapery and therefore is known as -pleated sheet.
O N C H
C H O N
O H
C N
C N C
O H O
H O N C H
N C H O N
 -pleated sheet structure of a protein

Q.12 Gabriel Phthalimide synthesis

Better yields are generally obtained by the gabriel phthalimide synthesis ; the  - halo esters are used
instead of  - halo acids .

O O
C C
+ – KCl
N¯ K + Cl–CH 2COOC2H5 N– CH2COOC2H5
C C
O O
Potasium
phthalimide HCl , H2O

+
Cl¯ H3N – CH2 COOH + phthalic acid
Glycine hydrochloride

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Q.13 Neutral - Amino acid having equal number of NH2 and COOH.
Neutral amino acids are further classified as polar and nonpolar depending on whether their side chains
have polar substituents (for example, asparagine with an NH2CO group) or are completely hydrocarbon
in nature (for example alanine, valine etc.).
Acidic -Amino acid having more COOH than NH2
Aspartic acid and glutamic acids, each with a second CO2H in their side chain are acidic amino acids.
Basic - Amino acid having more NH2 than COOH
Lysine, arginine and histidine, each with a basic site in their side chain are basic amino acids.

Q.14 Acidity and basicity constant are ridiculously low for –COOH and –NH2 groups. Glycine, for example,
has Ka = 1.6 × 10–10 and Kb = 2.5 × 10–12, whereas most carboxylic acids have Ka values of about
10–5 and most aliphatic amines have Kb values of about 10–4.
All these properties are quite consistent with a dipolar ion structure for the amino acids (I)
+
H3N–CH–COO¯
R
Amino acids : dipolar ions (Zwitter ion)

Q.15
(a) Denaturation of proteins
The process that brings about changes in physical as well as biological properties of proteins of proteins
is called denaturaion of protein.
Important features:
(i) It is caused by change in pH, temperature or by other denaturing agent like acid, alkali etc.
(ii) Denaturation does not change the primary structure of protein but the secondary & tertiary structure.
(iii) Denatured proteins lose its biological activity.
(iv) During denaturation ordered and specific conformation convert into uncoiled and random conformation,
so entropy increases during denaturation.
(v) Denaturation may or may not be reversible.
(b) What happens when a solution of an amino acid is placed in an electric field depends upon the acidity or
basicity of the solution.
+
H
+
 H 
H2NCHCOO¯ H3NCHCOO¯ H3NCHCOOH
OH¯ OH¯
R R R
Ka 2 Ka 1
(II) A (I) DI (III) C
In quite alkaline solution, anions (II) exceed cations (III), and there is a net migration of amino acid
toward the anode. In quite acidic solution, cations (III) are in excess, and there is a net migration of
amino acid toward the cathode. If (II) and (III) are exactly balanced, there is no net migration ; under
such conditions any one molecule exists as a positive ion and as a negative ion for exactly the same

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 B I O M O LE C U LE S

amount of time, and any small movement in the direction of one electrode is subsequently cancelled by
an equal movement back towards the other electrode. The hydrogen ion concentration of the solution
in which a particular amino acid does not migrate under the influence of an electric field is
called the isoelectric point (pI) of that amino acid. The isoelectric point (pI) is the pH at which
the amino acid exists only as a dipolar ion with net charge zero.
For glycine, for example, the isoelectric point is at pH 6.1.

EXERCISE-2
Q.1 D Q.2 A Q.3 D Q.4 B Q.5 A Q.6 A Q.7 B
Q.8 B Q.9 C Q.10 A Q.11 C Q.12 C Q.13 A Q.14 D
Q.15 B Q.16 A Q.17 C Q.18 A Q.19 D Q.20 A Q.21 A
Q.22 A Q.23 B Q.24 C Q.25 B Q.26 A Q.27 B Q.28 B
Q.29 B Q.30 B Q.31 D Q.32 C Q.33 C Q.34 B Q.35 B
Q.36 C Q.37 B Q.38 B Q.39 B Q.40 C Q.41 C Q.42 D
Q.43 A Q.44 D Q.45 B Q.46 B Q.47 C Q.48 A Q.49 C
Q.50 D Q.51 B Q.52 C Q.53 B Q.54 B Q.55 C Q.56 B
Q.57 C Q.58 B Q.59 C Q.60 C Q.61 C Q.62 C Q.63 B
Q.64 C Q.65 B Q.66 B Q.67 C Q.68  Q.69  Q.70 D
Q.71 B Q.72 B Q.73 A Q.74 C Q.75 B Q.76 C Q.77 D
Q.78 B Q.79 B Q.80 C Q.81  Q.82 C Q.83 B Q.84 B
Q.85 A Q.86 C Q.87 D Q.88 B Q.89 A Q.90 C Q.91 A
Q.92 A Q.93 A Q.94 C Q.95 A Q.96 B Q.97 C Q.98 A
Q.99 B Q.100 (i) B, (ii) D Q.101 B Q.102 B Q.103 C Q.104 A
Q.105 C Q.106 A Q.107 B Q.108 B Q.109 C Q.110 A Q.111 D
Q.112 A Q.113 C Q.114 A Q.115 B Q.116 B Q.117 B Q.118 A
Q.119 C Q.120 C Q.121 B Q.122 C Q.123 C Q.124 A Q.125 C
Q.126 C Q.127 B Q.128 C Q.129 C Q.130 C Q.131 D Q.132 C
Q.133 C Q.134 A Q.135 B Q.136 C Q.137 B Q.138 D Q.139 A
Q.140 D Q.141 D Q.142 B Q.143 A Q.144 C Q.145 A Q.146 D
Q.147 D Q.148 C Q.149 A Q.150 B Q.151 C Q.152 D Q.153 C
Q.154 D Q.155 ABCD Q.156 ABCD Q.157 AB Q.158 ABC Q.159 BCD Q.160 ABD
Q.161 BC Q.162 AB Q.163 ABCD Q.164 B Q.165 ACD Q.166 ABC Q.167 BCD
Q.168 A Q.169 (A) Q,S (B) S (C) R,S (D) Q, R,S
Q.170 (A) Q,S (B) Q,S (C) P,R,T,U (D) P,S,T,U Q.171 (A) QR (B) R (C) P (D) QR
Q.172 (A) P, (B) P (C) Q (D) Q Q.173 (A) P (B) Q (C) Q (D) R
Q.174 (A) P (B) PQR (C) QR Q.175 (A) PQS (B) PRS (C) QS
Q.176 (A) R, (B) P, (C) Q, (D) S Q.177 (A) S, (B) Q, (C) R, (D) P
Q.178 (A) S, (B) Q, (C) R, (D) P Q.179 (A) Q, (B) R, (C) S (D) P

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Q.180 (A) S (B) P, (C) R, (D) Q, (E) T Q.181 (A) S, (B) R, (C) T, (D) P, (D) Q
Q.182 (A) R, (B) Q, (C) S, (D) P Q.183 (A) S, (B) R, (C) T, (D) P, (E) Q

EXERCISE-3
SECTION-A

CH2OH
CHO
H OH C=O
HO H HO H
Q.1 H OH H OH
H OH H OH
CH2OH CH2OH
Glucose + Frucose

Q.2 (i)Amine, carboxylic acid,Amide, Ester

O
NH–C COOH

Q.3 H2 N COOH

NH2 O

HOOC NH–C COOH

CHO COO
HO H HO H
+
H OH [Ag(NH 3) 2] H OH
Q.4 HO H HO H
HO H HO H
HO HO
L - Glucose

Q.5 B Q.6 B Q.7 D Q.8 A Q.9 D

Q.10 (A) P,S; (B) Q, R; (C) P, R; (D) PRS Q.11 A Q.12 BC Q.13 D Q.14 A
Q.15 B Q.16 6 Q.17 4 Q.18 8 Q.19 4 Q.20 1 Q.21 A
Q.22 BC Q.23 D
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SECTION-B
Q.1 A Q.2 A Q.3 A Q.4 A Q.5 A Q.6 B Q.7 D
Q.8 D Q.9 B Q.10 C Q.11 A Q.12  Q.13 C Q.14 D
Q.15 A Q.16 D Q.17 D Q.18 D Q.19 D Q.20 C

EXERCISE-4
Q.1 Hormones are complex organic compounds which are produced in endocrine glands and are directly
secreted into blood stream. These control the various metabolic processes.
(i) Testosterone controls normal function of male sex organs.
(ii) Oxytocin responsible for signaling contraction of the womb in woman during labor. The hormones
stimulates the utersine muscles to contract, so labor begins. It increases production of prostaglandins
which move labor along and increases the contraction even more. It promotes lactation by moving the
milk into the breast oxytocin secreation causes the milk to relaease so the baby can feed.

Q.2 Replication is the process by which a single DNA molecule produces two identical copies of itself,
during cell division. During this process, the two strands of the double helix first separate and each
separated strand then serves as a template for the synthesis of new strand. Due to specificity of base-
pair, the sequence in the two new strands is complementary to the original. In other words, replication
leads to the production of two identical copies of DNA from a single parent DNA and copy of each then
passes on the new cells resulting from cell division. In this way, the hereditary effect are transmitted from
one cell to another.
T T

G C

A T

C G

T A

C G C G
A T A T
G C G C
C G C G
T A T A

Q.3 On the basis of hydrolysis, carbohydrates can be divided in three major classes :
(i) Monosaccharides : They cannot be hydrolyse into simpler molecules. They are further classified as
aldoses and ketose.
(ii) Oligosaccharides : These carbohydrates on hydrolysis give 2-10 monosaccharides. For example,
sucrose.

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(iii) Polysaccharides : These are high molecular mass carbohydrates which give many molecules of
monosaccharide on hydrolysis. For example starch and cellulose.

Q.4 (a) (i) HOCH2 – (CHOH)4 – CHO + 5 (CH3 CO)2 O

Glucose Acetic anhydride
 OHC – (CHOCOCH3)4 – CH2OOCH3
Pentaacetyl glucose
(ii) Glucose reduces ammonical silver nitrate solution (Tollen's reagent) to metallic silver.
HOCH2 – (CHOH)4 – CHO + Ag2.O
 HOCH2 – (CHOH)4 – COOH + 2 Ag
Glucose acid
(b) Replication is the process by which a single DNA molecule produces two identical copies of itself,
during cell division. During the process, two strands of the double-helix first separate and each separated
strand then serves as a template for the synthesis of new strand. Due to specificity of base pair, the
sequence in the two new strands is complimentary to the original .
The structural differences between DNA and RNA are
(i) DNA has -D-2-deoxyribose sugar while RNA has -D-ribose sugar
(ii) DNA contains thymine and RNA has uracil
(iii) DNA is double stranded while RNA is single stranded

Q.5 (a) Vitamin can be defined as the essentials dietary factors required byan organisms in minute quantities
and whose absence causes specific deficiency diseases.
Vitamins are broadly classified into two types :
1. Fat soluble vitamin : These are oily substances not readily soluble in water. These include vitamins
A, D, E and K, B12
2. Water soluble vitamins : The vitamin B and C are water soluble and are stored in much smaller
amounts in the cells.
Vitamin H also known as B7 (Biotin) is an exception, it is neither soluble in water nor in fat.
(b) Enzymes are naturallyoccurring simple conjugate proteins actingas specific catalysts in all processes.
In contrast to ordinary chemical catalyst, it loses activity by pH or temperature change.
Enzymes are highlyspecific, i.e., a particular enzyme catalyses a specific reaction. For example urease
attacks on urea. This specific action is due to active sites present in the enzyme molecule (E) that fits
into substrate (S) and forms E-S complex which changes into product P and E.
For example
NH4CONH2 + H2O Urease
  CO2 + 2 NH3
Urea

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Q.6 (a) (i) CHO CH = N – OH

NH2OH
(CHOH)4 (CHOH)4

CH2OH CH2OH
Glucose Glucose monoxime

(CH3CO)2O
(ii) OHC – (CHOH) 4¯ CH 2OH
Glucose
OHC – (CHOCOCH 3) 4 – CH 2OOCCH 3
Pentacetate

Name of Vitamin Food Source Deficiency Disease

Vitamin-A Fish oil, Liver Hardening of cornea of eye

(b) Vitamin-C Citrus fruits, Green vegetables Scurvy

Vitamin-E Wheat germ oil, Cotton Seed oil Steritity

Vitamin-K Cereals, Leafy vegetables Hemorrhagic condition

Q.7 Functions of nucleic acid : (i) RNA acts as an intermediatry compound in the synthesis of proteins from
the genetic codes of DNA. Molecules of RNA being specific amino acids to the ribosomes for
incorporation into the protein.
(ii) DNA contains the genetic information of a particular species and passes on the same by a process
named replication. It takes part in the synthesis of RNA by the process named transcription.

Q.8 A copolymer is formed by the polymerisation of two or more than two different monomers.
Yes, a copolymer can be formed in both addition and condensation polymerisation. For example
(i) The addition polymerisation of styrene and butadiene forms a copolymer styrene-butadiene rubber
(addition polymerisation)

n CH2 = CH – CH = CH2 + n C6H5 CH = CH2

C6H5

( CH2 – CH = CH – CH2 – CH2 – CH ) n

(ii) The condensation polymerisation of hexamethylenediamine and adipic acid form a copolymer
nylon-66
HOOC (CH2)4 COOH + NH2 + (CH2)6 NH2  ( NH (CH2)4 NHCO (CH2)2 CO ) n

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Q.9 Nucleotides : There are the monomeric units of a type of long polymers called nucleic acids. These are
compound of three components viz. nitrogen containing heterocylic base, a five carbon sugar and a
phosphoric acid moiety.

Nitrogen containing bases

Purines and pyridines

Q.10 Allergic response produced in the body :Allergy in a state of hypersensitivity characterized by difficult
respiration and skin rashes. The substances that cause allergy is called allergin. When these come in
contact with a cell to which a particular type of antibody is attached, antibody - antigen complex is
formed. The formation of the later leads to the release of allergy mediators which are responsible for
various allergysymptoms.
Antithistamine : These are the drugs used to treat allergy. These drugs act by blocking, one specific
type of allergy mediator called histamine.

Q.11 (a) Digestion : Digestion is a process in which complex nutrient molecules such as fats, proteins, starch,
carbohydrates etc. are converted into simple nutrient molecules by the action of enzyme secreted by the
wall of the digestive tract.
Digestion of carbohydrates : Carbohydrates are class of compounds which include polyhydroxyaldehydes,
polyhydroxyketones and large polymeric molecules. In the digestive tract, the carbohydrate is ultimately
converted into monosaccharide (e.g. fructose, galactose and glucose) by the action of enzyme amylase,
secreted by saliva and the walls of intestine. Glucose is absorbed by the blood and get stored in liver
and muscles. The glucose burns in cells to liberate energy.

Q.12 (a) These are amino acids which are essential for maintenance of proper nitrogen balance in the body but
cannot be synthesised within living organisms. Out of 20 amino acids that make up protein , 10 are
synthesised by our bodies (non-essential amino acids) and other 10 amino acids known as essential
amino acids must be supplied in the diet through protein-rich diets like milk, fish eggs, meat, bean and
peas.
(b) Photosynthesis : It is a series of complex biochemical reaction involving two stages :
(i) Light reactions : These reactions occur in the presence of sunlight. The sunlight is absorbed by the
chlorophyll of plant cells. This energy is used to synthesis energyrichATP molecules with the liberation
of oxygen.

 hv
H2O + CO2 Chlorophyl Organic molecules + O2 + ATP
l

(ii) Dark reactions : These reactions takes place in the absence of light but immediately after light
period. The energy ofATP molecules is used in the conversion of CO2 of the atmosphere into glucose
and then into starch.
6CO 2  6H 2 O ATP
 C 6 H12 O 6  6CO 2

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The synthesis of each molecule of glucose consumes 18 molecules ofATP.

(c) The two main products of glycolysis are pyruvate (a 3-carbon molecule) andATP molecules.

Q.13 Reducing sugar : D-fructose Nonreducing sugar : Sucrose

Q.14 (i) The digestion of protein begins in the stomach which contains the enzyme pepsin. The digestion
continues in the intestine in presence of trypsin, chytrypsin and various other peptidases secreted by
pancreas and intestine. During digestion the proteins are converted into -amino acids by breaking
peptide linkage which are absorbed by blood.
(ii) Different types of RNA founds in cells are
(a) Messenger RNA : It carries the genetic code form DNA to ribosomes where protein is synthesised.
(b) Ribosomal RNA : It is present in ribosomes. It function is to provide the site for protein synthesis.
It helps in binding m-RNA to ribosomes during protein synthesis.
(c) Transfer RNA: It transfers amino acids from different parts of cytoplasm to the ribosomes during
protein synthesis.

Q.15 Adenine and Guanine.

Q.16 (a) Polymers are classified on the basis they are naturally occurring or synthetic. Some of the natural
polymers are starch, cellulose, proteins and nucleic acids etc. Synthetic polymers are man-made
polymers such as polyethylene, PVC, teflon, nylon etc.
(b) It has been observed that there are some organic compounds other than carbohydrates, proteins
and fats which are necessary for normal growth and maintenance of health. These specific organic
compounds are known as vitamins. Theyare classified into two broad types based on their solubility in
fats and water.
Vitamin A, D and K are fat soluble where as vitamin of B group such as B1, B6, B12 and vitamin C are
water soluble.

Q.17 (a) Based on structure, the carbohydrate have been classified into three main classes.
(i) Monosaccharide
Examples : Glucose, Fructose
(ii) Diasaccharides
Example : Maltose , Sucrose
(iii) Polysaccharides
Example : Starch, glycogen
(b)
(i) The primary structure of a protein determines its functions and biological activity.
(ii) Protein synthesis takes place in ribosomes.

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Q.18 Because the electron pair of nitrogen can conjugate with the benzene ring giving carbon nitrogen bond
with double bond character.

Q.19 B-complex is a group of vitamins contains vitamins B1, B2, B6, B12, biotin, folic acid, pantothenic acid
and nicotinic acid. It is required to release energy from food and to promote healthy skin and muscles. Its
deficiency causes beriberi and pernicious anaemia.

Q.20 (a) (i) Reducing sugars :All those carbohydrates which reduce Fehling's solution and Tollen's reagent
are called reducing [Link] monosaccharide are reducing sugars in nature.
(ii) Denaturation of protein : The complex three-dimensional structure of proteins gets distributed by
changing the pH, temperature or by adding some salt. This disruption of the native structure of protein
is called denaturation of protein.
(iii) Oxygen is replenished in out atmosphere through photosynthesis in plants.
(b) Enzymes : Most of the chemical reactions which occur in living systems process at very high rates
even under mild conditions of temperature and pH. These reactions are catalysed by a group of
biomolecules called enzymes.

Q.21 Peptide Linkage : Proteins are condensation polymers of -amino acids in which the same or different
-amino acids are connected by peptide bonds. Chemically, a peptide bond is an amide linkage formed
between – COOH group of one -amino acid and NH2 group of the other -amino acid by loss of a
molecule of water.

Q.22 Main functions of carbohydrates in plants :

(i) Carbohydrate are used as storage molecules as starch in plants.
(ii) Cell wall of bacteria and plants is made up of cellulose

Q.23 (i) On prolonged heating with HI, D-glucose forms n-hexane.

CHO
HI, 
(CHOH)4 CH3 – CH2 – CH2 – CH2 – CH2 – CH3
n–Hexane
CH2OH
D-Glucose
(ii) D-glucose gets oxidised to six carbon carboxylic acid (gluconic acid) on reaction with bromine
water
CHO
Br2 water
(CHOH)4 COOH

CH2OH (CHOH)4
D-Glucose
CH2OH
Gluconic acid

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(iii) On oxidation with nitric acid, D-Glucose yields a saccharic acid

CHO COOH
HNO3
(CHOH)4 (CHOH)4
Oxidation
CH2OH COOH
D-Glucose D-saccharide acid

Q.24 Classification of Vitamins : Vitamins are classified into two groups depending upon their solubility in
water or fat.
(i) Fat soluble vitamins
(ii) Water soluble vitamins
Sources of VitaminA: Fish liver oil, carrots, butter and milk.
Sources of Vitamin C : Citrus fruits, amla and green leafy vegetables.

Q.25 The drug attachment of natural substrate on active site on an enzyme can be prevented by two ways :
(i) Catalytic action of enzymes (ii) Drugenzyme interaction

Q.26 Amino acids :Amino acids contains amino (–NH2) and Carboxyl (–COOH) functional groups. Depending
upon the relative position of amino group with respect to carboxyl group, the amino acid can be classified
as , , ,  and so on.
In acidic medium , -amino acids exist as cation (I) and thus migrate towards cathode under the
influence of an electric field.
On the other hand, in alkaline medium, -amino acids exists as anions (II) and thus migrate towards
anode under the influence of an electric field.

Q.27 Essential amino acids : -amino acids which are needed for health and growth of human beings but
are not synthesised by the human body are called essential amino acids.
Examples : Valine, Leucine etc.
Non-Essential amino acids : -amino acids which are needed for health and growth of human being and
synthesised by the human body are called non-essential amino acids.
Example : Glycine, aspartic acid etc.

Q.28 Biomolecule Type of linkages

1. Primary structure of proteins Peptide bond or peptide linkage
2. Cross-linking of polypeptide chains Polypeptide linkage
3. -helix formation Hydrogen bonds
4. -sheet structure Intermolecular hydrogen bonds.

Q.29 Example of water soluble vitamin : B group vitamins and vitamin C.

Name of vitamins Sources Deficiency
Vitamin B1 Yeast, milk, green Beri-beri
vegetables and cereals
Vitamin C Citrus fruits, amla and Scurvy(Bleeding gums)
green leafy vegetable

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Q.30 (a) Nucleotide is formed by condensation of a purine or pyrimidine base with Pentose sugar at position
1. When nucleoside is linked to phosphoric acid at 5' position of sugar moiety, we get a nucleotide.
(i) Nucleoside has two units : Pentose sugar and a base.
(ii) Nucleotide has three units : Phosphate group, pentose sugar and a base.

O
5' O 5' O
HO – H2C Base O – P – O – H2 C Base
4' H 1' 4' H 1'
H O H
H 3' 2' H H 3' 2' H
OH OH OH OH
Nucleoside Nucleotide

(b) DNA is a double helix in which the two strands of DNA are held by the hydrogen bonds between the
bases on the two strands. Thymine (T) pairs with adenine through two hydrogen bonds and cystosine
(C) pairs with guanine (G) through three hydrogen bonds.

So opposite each adenine (A) on one strand there is always a thymine on the other strand and opposite
guanine there is cytosine.
Hence the two strands of DNA are complementary to each other.

Q.31 During denaturating , the protein molecule uncoils from an ordered and specific conformation into a
more random conformation. Denaturation does not change the primary structure of protein.

Q.32 (i) Food preservation : Food preservation are the substances used to prevent spoiloge of food due to
microbial growth during storage. The most common preservation used are table salt, vegetable oils and
sodium benzoate (C6H6COONa)
(ii) Enzymes : The proteins which perform the role of biological catalysts in the body are called
enzymes. Examples : E. coli.
(iii) Detergents : Detergents may be defined as ammonium, sulphate or hydrogen sulphate salts of long
chain hydrocarbons containing 12-18 carbon atoms.
Example : The more common detergents are the sodium salts of long chain sulphonic acids.

Q.33 Fibrous Protein Globular proteins

(i) When the polypeptide chains run parallel (i) when the chains of polypeptide coil
and are held together by hydrogen and around to give a spherical shape
disulphide bonds to give a fibre like
structure
(ii) They are generallyinsoluble in water (ii) They are usually soluble in water
Example : Keratin and myosin Example : Insulin and albumins

Q.34 (a) -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 to the helix.

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(b)
Globular proteins Fibrous proteins
(i) These proteins are cross linked These are linear condensation product
condensation product of basic
and acid amino acids
(ii) These are soluble in water or aqueous These are insoluble in common solvent
solution of acids, bases or salts. but soluble in strong acids and bases
(iii) Examples of globular proteins are Example are myosin in muscles, keratin
albumines in egg; all enzymes and in hair and fibroin in silk.
hormones

Q.35 Vitamin : The organic compounds which cannot be produced by the bodyand must be supplied in small
amounts in diet to perform specific biological functions for the normal health, growth and maintenance
body is called vitamins.
(i) Pernicious anaemia is caused by the deficiency of vitamin B12
(ii) Convulsion is caused by the deficiencyof vitamin B6

O
1 1
H – C – OH 1 H–C–H
H–C
2 2 2
H OH H OH H OH
3 O 3 3 O
HO H HO H HO H
4 4 4
H OH H OH H OH
Q.36 5 5 5
H H OH H
6 6 6
CH2OH CH2OH CH2OH
-D–(+)–Glucose -D–(+)–Glucose

Glucose is found to exist in two different crystalline form which are named as  and . The -form of
glucose (m.p. 419 K) is obtained by crystallisation from concentrated solution of glucose at 303 K
while the -form (m.p. 423 K) is obtained by crystallisation from hot and saturated aqueous solution at
371 K.

Q.37 (i) Disaccharide on hydrolysis with dilute acids or enzymes yield two molecules of either the same or
different monosaccharides. The two monosaccharides are joined together by an oxide linkage formed
by the loss of a water molecule. Such a linkage between two monosaccharides units through oxygen
atom is called glycosidic linkage. Proteins are the polymers of -amino acids and they are connected to
each other by peptide bond or peptide linkage. Chemically, peptide linkage is an amide formed between
–COOH group and – NH2 group.

Q.38 DNA contains a five carbon sugar molecules called deoxyribose whereas RNA contains ribose. Both
DNA and RNA contain adenine, guanine and cytosine. The fourth base is thymine in DNA and uracil in
RNA. The structure of DNA is double strand whereas RNA is a single strand molecules. DNA is the
chemical basis of heredity and have the coded message for proteins to be synthesised in the cell.

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Q.39 RNA : (Ribonucleic acids) contains the sugar D-ribose. The base thymine is never present in it. Its
molecule consists of a single strand. It is mainly formed in the cytoplasm in the cell. It does not self-
replicate.

Q.40 D-Glucose and D-Galactose

Q.41 2 glucose molecules.

Q.42 (i) The linkage between two monosaccharide units through oxygen atom is called glycosidic linkage.

CH2OH
O H
H O H
H
O
OH H H OH CH OH
OH 2

H OH OH H
Glycosidic linkage

(ii) Invert Sugar :An equimolar mixture of D – (–) glucose and D–(–) fructose, obtained by hydrolysis
of sucrose in presence of an acid such as dil HCl or the enzyme invertase or sucrase.
(iii) Oligosaccharides : These are carbohydrates which on hydrolysis give two to ten molecules of
monosaccarides, Depending upon the number of monosaccharides molecules actually obtained upon
hydrolysis, they are futher classified as di, tri, tetrasaccharides etc.

Q.43 (i) Maltose

(ii) Acidic amino acid has more COOH group
Basic amino acid has more NH2 group
(iii) Phophodiester bond

Q.44 (i) D-glucose exist in two anomeric forms, in cyclic and open chain structure
It has following drawbacks in cyclic form.
(a) It does not form addition compound with NaHSO3, NH3 and Grignard reagent, thus
indicating absence of CHO group
(b) It does not give Schiff's test
(ii) Phosphodiester linkage is present in Nucleic acid.
(iii) Water soluble :  Vitamin B, Vitamin C
and Fat soluble : Vitamin A, Vitamin D, Vitamin E

EXERCISE-5
Q.1 A Q.2 A Q.3 A Q.4 C Q.5 B Q.6 D Q.7 B
Q.8 B Q.9 C Q.10 D Q.11 A Q.12 D Q.13 C
Q.14 ABCD Q.15 ACD Q.16 ABCD Q.17 ABCD Q.18 ABCD Q.19 ABC
Q.20 (A) P,Q,R (B) P (C) P (D) P,Q,R Q.21 (A) PQ (B) P (C) RS
Q.22 (A) R, (B) P (C) P (D) P (E) P Q.23 (A) Q (B) P (C) R (D) S
Q.24 3.25
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NOTES

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