BIOMOLEcULES 01

A Iving systems are made up of non-living atoms and molecules. The study of 'what goes on chemically in a living system' is a vast field
caed Biocnemistry,ompiex organic moiecues which Dund up lIiving organisms and are required for growth and maintenance of the
Dody, are called biomolecules. hus, compounds like proteins, enzymes, hormones, vitamins, nucleic aids, carbohydrates, fats, lipids
etcare all biomolecules. Many of them are polymers with high MWs. Living beings either take them in the form of food or prepare them
in their bodies. Many complex reactions take place in living systems with the heip of highly specific biocatalysts called enzymes. These
chemical reactions, which are called metabolic pathways, take place in dilute solutions, at body pH and at one atm pressure.
Carbohydrates, fats and proteins are the main constituents of food. Structures and functions of some biornolecules are given below :
CARBOHYDRATES
Carbohydrales are naturally occurring organic compounds produced by plants. They consist of C, H and O only and in many of then,
ratio between number of H and O atoms is same as in water i.e., 2:1. Thus, their general formula is C{H0)y and they were considered
as the hydrates of carbon e.g glucose [CoHi20o) can be written as Co(HaO)a. That is how the term "carbohydrate' was derived. But all
those compounds which correspond to the general formula C(H20)» are not carbohydrates e.g., HCHO, CHCOOH, Lactic acid etc
Similanly, all carbohydrates do not correspond to this formula e.g., thamnose (CoH120s).
On the basis of chemical reactions, carbohydrates are found to contain some specific functional groups. Thus, chemically they are defined
asOptically active polyhydroxy aldehydes or polyhydroxy ketones and also those compounds which produce them on
ny arolystS. Some carbonyrates are aiso called Saccharides because they are sweet e.g., GlucOse, sucrose etc.
Carbolhydrates constitute 70% of the solid plant material. Their main functions are
01 to support plant structure (cellulose),
02 to store chemical energy (sugar and starch).
Carbohydrates are present in all basic necessities of life i.e., food, clothing and shelter (wood for furniture and construction).
CLASSIFICATION OF CARBOHYDRATES
A classification Based on the Number of Products obtained on Hydrolysis :
01 Monosaccharides: These are the carbohydrates which do not split into.smaller units on hydrolysis
ie., they do not hydrolyze
e.g9ucose, ructose etc. About 20 monosaccharides occur in nature. They are crystalline, sweet in taste, soluble in water
anoChar on heating. hey contain minimum three carbon atoms.
02 Oligosaccharides : (oligos=few) These are the
carbohydrates which split into a few but a definite number (2 to 10) of smaller
on
monosaccharde units hydrolysis. They are further classified as disaccharides, trisaccharides, etc., depending on the number
hey provide on hydrolysis eg.
Omonosacchande unts Sucrose is a disaccharide which gives glucose and fructose on
;
nydroiysis tartinose Is a trisaccharide which gjives glucose, fructose and galactose on hydrolysis.
wO monosacchanideunits obtained by the hydrolysis of a disaccharide may be same (e.g., maltose gives two molecules of
glucose) or dferent (e.g., sucrose glves one molecule each of glucose and fructose)
03 Polysacharidas These are high MW carbohydrates which splt into many smaller (CooOsn+ nH:0HnCoH20
monosacchande units on hydrolysis e.g, starch, cellulose, glcogens, gums etc. starch/cellulose Glucose
BClassifcation Based on Taste All monosaccharides anddisaccharides are crystalline solids, soluble in water and sweet in taste
:
and ar calied augars while poysacchandes are amorphous, insoluble in water and not sweet in taste and thus called non-sugars.
C Classification Based on the Reaction with Tollen's Reagent: Those arbohydrates which can reduce Tollen's
reagent/ Fehling
solulion, are called reducing carbohydrates I reducing sugars while those which cannot reduce them, are called non-reducing
sugars/non-reducing carbohydrates.
All monosaccharides have free aldehydic or ketonic group due to which they are reducing sugars carbohydrates. All
sugare /carbobydrates because they do not have free aldehydic or ketonic group. Dísacchrides
poly saccharide ar nonreducing
may or may not be reducing sugars (see disaccharides)
MONOSACCHARIDES
A Classification of Mono3accharides Based on Carbonyl Group
|01Aldoses: Carbohydrates which contain aldehydic group are called aldoses e.g. glucOse, ribose etc.
keto group are called ketosas e.g, dihydroxyacetone, fructose, etc.
02 Ketoses: Carbohydrates which contain on
BClassification of Mono8accharides Based Number of Carbon Atoms:
01 Trioses: These are the carbohydrates which contain three carbon atoms e.g, 9yceraldehydes, dihydroxyacetone etc.
02 Tetroses: These are the carbohydrates which contain four carbon atoms e.g., erytherose etc.
03 Pentoses: These are the carbohydrates which contain five carbon atoms e.9, ribose etc.
04 Hexoses: These are the carbohydrates which contain sbx carbon atoms eg, glucose, fructose ete.
1. GLUCOsEDEXTROsE/GRAPE SUOAR/CH0,
Glucose ocCurs in nature in free Bs well 8s combined 1orm. it 1s present In fruits and honey, Ripe grapes contain approx 20%
glucose.
Preparaton of Glucose : Commerclally, Itls prepared by the following methods:
01 From Sucroselcane sugar: When sucrose ls bolled with dlute HCl or H2804 CiaHzO11 +
H20 CuHi20a CotiaOs
in aiconolic soluUon, gluco56 and iructOBe are oblained in equimolar amount.
02 From Starch : When starch ls boiled with dilute H2804 at 383 K and hlgh (CoHio0s)n+nHa0 He
pressure, glucose ls obtalned. S nCaH120s
Starchcellulose Glucose
Structure OF Glucos0: Glucose ls an aldohexose because It has sbx carbon atoms and aldehydic group. It is
monomer also called dextrose
because it ls dextrorotatory. ls a
It
ofa large number of polysaccharides like starch cellulose etc. It ls the most abundant organic
compound on earth. 1ts structure 1s based o1 following evidences

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 OMOLR
BIOMOLECULES 02
A Open Chain Structure of Glucose:
01 1ts molecular formula was found to be CoH1206.
02 On heating with HI for a long time, it forms n-hexane 03 Glucose reacts with hydroxylamine (NH2OH) to form an oxime.
which proves that all the six C-atoms in glucOse are AIso, with HCN, it forms cyanohydrin. These reactions confirm
arrangedin a stralght chain. the presence of a carbornyl group PC 0) in glucose.
CH=N-OH
HO CHO CHOH(CN)
CHOH) n-Hexane CHOH) O (CHOH)HC (ÇHOH)
CH:OH CH:OH (onme
CHOH coe) CH:0R Cyarn
04 4. Glucose is oxidized to gluconic acid by mild 05| 5. Acetylation of glucose with acetic anhydride gives glucose
oxidizing agents like Tollen's reagent, Fehling's pentaacetate which confirms the presence of five -OH groups
solution and bromine water. This indicates that the which should be attached to different carbon atoms.
carbonyl group present is as an aldehydic group.
CHO coOH CHO
HO
(ÇHOH)4Tolen's regon CHOH) (CHOHJ4+ 5(CH»CO)20 (CH-O-co-CHj4 +5CHCOOH
CH2OH CH2OH (Gonc acd CH2OH CHa-0-CO-CHs (Gucose pentaacatate)
06 Oxldation of glucose as well as gluconic acid with nitric HO oOH COOH
acid gives a dicarboxylic acid, Sacchanc aca CHOH)4 9sdan (ÇHOH}%
len (ÇHOH)4

9COOR
e S
Conns presence ora pnmay aconoC group
e wnicn oxCZe to gropecont COOH CH2OH
grOup comes trom oxidabon of-GHO group
he slucose Saccharic acid Gluconic acid
Exact arrangement of fveOH groups in 3D was given by CHO COOH poOH
FIScher on the basis of many other properties. This OH H OH
conhguration is gven alongside. On the basis of HO HH
HO HO -H
conhguration of glucose, contgurations of gluconic acid -OH OH
and sacchanc acid are also given. OH H OH OH
CH2OH CH2OH COOH
Glucose Gluconic acid Saccharic acia
cComplete name of glucose is D-(glucose where 'D' represents configuration and () represents dextrorotatory nature of glucose.
D nas no reiauon win opucal acIVIy OT tne compound. Meaning otD- (or L-) notations to represent coniguraion Is grven beiow
D-(or L-) confguration in comparison with two enantiomers of gyceraldehyde as shown alongside CHO
one H OH
ASshown.iyceraldehyde has asymmetric C-atom. fOH group on this C-atom is on the RHS, is it
CH2OH
assigned 'D' configuration and ff-OH group is on the LHS, R Is assigned 'L coniguraton.
D-Gyceraldetyda
To assign configuration to a monosaccharide, its most oxidized C-atom is held on the top and the lowest CHO
asymmetnc C-atom is compared with above two enantiomers of gyceraldehyde. If-OH group on the lowest HOetHOoH
asymmetric C-atom is on the RHS, monosaccharide is assigned D-configuration e.g., in D-(-glucose,
-OH group on the lowest asymmetric carbon (.e., Co) is on the RHS. LGlyceraldehyde
Byclic Structure of Glucose :
Open chain structure of glucose explains most of its properties except but following observations
01 Although glucose has -cHO group but it does not give 2,4-DNPH test, Schiff's test and it does not react w
aHSOs
Glucose pentaacetate does not react with hydroxylamine indicating the absence of free-CHO group.
02
| 03Glucose exists in wo foms called a- and -Glucose. Diferences between these two foms of glucose are given below:
a-Glucose B-Glucose
Crystallzes a
from cold & conc aqueoUs solution at 30 G. | Crystallizes from hot & conc aqueous solution at 98 C.
"Melting point=419K Melting point=423 K.
Optical rotation of freshly prepared solution is 111. Optical rotation of freshly prepared solution is 19.2.
w
Its polymer (starch) is easily digested by humans. lts polymer (cellulose) is not digested by humans.
04
a
solution of either of the two forms is dissolved
and ultimately becomes constant at 52.50, This
h in water
andter if a to stand, optical rotation
allowed of the solution slowty changes
or base Is added to the solution.
Such a spontaneous change in optical rotation of a compound is called Mutarotation.
These observatons can be explained on the basls of cyalle hemlacetal structure of glucose which is fomed by self condensation
con
Oatom.
bewe
That C-atomof
roun an
the ring which comes
C6
t
from-CHO c
atructre has six atoms in he ring out of which five
group of the open chain structure, is called anomeric
ae
C-atoms and one is
C-atom.-OH
onthis ctomhas wo ypes.of onentations a9 shown below and these orlentations correspond to a- and p-Glucose which are called
group

anomers. Thus, anomers are two differont 3D otructuros of glucoso whlch dliffor In thelr stereochemlstry at C-1

gHON
ON
HO-

-o
H--
CHON GHOH CHOH
Pischer Projection of a| Haworth structure of Pyran Fischer Projection of pHaworth structure of
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 Fischer projections for a- and B-Glucose are
BIOMOLECULES
03
not mirror images of each other and therefore, they are not optical isomers. Like this
structure of glucose, compound Pyran also has Tive carbon and one oxygen atom in the ring as given above. That is why, cyclic
atructure of glucose is called the Pyranose structure in analogy with Pyran.
Cycle stnucture of glucose was confirmed by R. D. Howarth. In Howarth representation, atoms/groups on the right hand side of
BChers projections are represented below the plane of the ring while atoms/groups on the left hand side of Fischer's projections
are represented above the plane of the ring. Thus, in a-Glucose, -OH groups on G-1 and C-2 are on the same side while in B-
GCOsSe,they are on the opposite sides.
Reason for Mutarotation: When either of the two forms is dissolved a-Glucose Open chain Glucose = -Glucose
n water, nmg opens upP, one torm changes into the other and tollowing9 (36%) (0.0276) (64%)
equnnornunm 1s established whose net oplical rotatlon is 52.5
2. FRUCTOSE/C;Hi0

ructose Is a ketohexose which is obtained HO HOHC -OH HOHC 0 CH,OH

ongwitn Glucose by the hydrolysis of sucrose.
Molecular fomula of Fructose is CoH120s. On HO H
the DasisHO H
rta reactions, its open chain structure is found to
contain a ketonic functional group at C-2 and nas a H
H O

stralght chain of six carbon atoms. Its contiguration is CHOH OH

D and is a laevorotatory compound. Thus, fructose is
CHOH
approprately written as D--Fructose. FIscher Projection d-U Fructorurarnose Haworth structure

It also exists in two cyclic forms which are formed by

the self condensation reaction betweenoH HO--CH-O HOM C

and carbonyl group at C-2. he

at
ing thus tormed
C-s HO

H OH
consists of four carbon and one oxygen atom. This is
H
caled furanose structure in analogy with the CH,OH OH
compound furan which has four, carbon and one Furan
oxygenatom inthe ning as given below. FischerProjection B-D-(-HFructofuranosee Haworth structure
DISACCHARIDES
hey are condensation producls of vo monosaccharide units whose hemiacetal structures are linked together through oxide linkage
aed gycosd inkage s
which fomed by the loss of a molecule of water. Thatis why, they produce two molecules of the same
or different monosaccharides on hydrolysis in the presence of an acid or an enzyme.
aacchandesmay be reducing or non-reducing sugars depending on the positilon of linkage of monosaccharides. If carbony! C-atom
both monosac charides are invoved in gcosidic linkage, disaccharide is a non-reducing sugar e.g. sucrose. If carbonyl group of one
s
monosacchanide is invoved in gycosidic linkage and the other free, then the disaccharides is a reducing sugar eg, maltose and lactose
01 8UCROSEeanesugarsuGARCH0 is the most common disaccharide found in plants which is manufactured from
Sugarcane or beet root. It is colourless, crystalline, sweet, water soluble and oauon of *66.5. Sucrose is a non-
C-atoms of units (C.1 of olucnseland
eoucing sugar because
reducing carbonyl C-atoms
because carbonyl both the unts
of both
the (G1 of gucOse) and (G2 o iructose) are nvolved in giycosidic linkage.
On bydrobysls in the presence di acid the enzyme invertase. CraHarO1 H:0 eraaren Ye
or H CoHzos+Cath20s
t ofa
gives equimolar mixture of D-HGIucose and DHeFructose. Sucro8e D4+)Glu D4Fru
Optical rotations of D-(+)-Glucose is (+ 52.5] while optical rotation of D---Fructose -92.4) Since laevorotation of fructose is more
than the dextrorotation of glucose produced, the mxture on the whole is laevorotatory whereas optical rotaton of starting sucrose is
+66.5. Thus, hydrolysis of sucrose leads to change in sign of optical rotation from dextro (+) to laevoF, such a change is called
inversion or Bugar and tne mixture of producis obtained is called invert sugar.
Fementation of sugarsolutlon in the presence of yeast (which provides enzymes) gives ethanol and carbon dioxide.
CiaH22011+ H0 CHi20s CeHi2Oe 4CaHsOH+ 4CO2
02 LACTOSEMILK SUGAR/CaHzaO t is found in milk. It is hydrolyzed in the presence of enzyme emulsin or dilute
acid and
an equimolar mixture of B-D-Galactose and p-D-Glucose. It has glycosidic linkage between C-1 of Galactose and C-4 of gives
Glucose
50 that carbonyi group ot Glucose is stll free due to which it is a reducing sugar.
MALTOSEMALT SUGARICHa0« t is prepared by partial hydrolysis of starch in the presence of enzyme
diastase, present in
mat (sprouted barey seeds).
2(CeH1oOs)n (Barech)+ nHaO nCiaHaaO11 (Maltose)
gives two molecules of a-D-(+)-Glucose on hydrolysls. In maltose, carbonyl group at
It
C1 of one unit foms gtycosidic linkage
with-OH group at C4 of the other unit so that carbonyy group on one unit is stil free. Due to this maltose a reducing sugar.
is
POLYSACCHARIDES
These are the carbohydrates which contalna large number of monosaccharlde units (hundreds or even thousands)
glycosldic linkages. They are amorphous 8olids, Insoluble In water, tasteless and therefore joined together by
called non-sugarS. They mainly act as food
storage or structural materals. Starch, cellulose, glycogen and dextrin are some important polysaccharides.
BIOMOLECULES
01 STARCHIAMYLUM(CaH40n) 1
a polysaccharide of a-D-()-Glucose. It ls present In plants and acts as a food reserve. It
It lo
human beings. Its main source 18 Seeds lIKe wheat, Ic8, maiz0, potatoe8, Dariey etc. t occus in
is the most important dietry source for
BZe and shape depending upon tne plant. A BuBpension or Btarch in water the tom ot granules which vary in
heating and reappears on cooling..
gives Due colour win lodine wnicn disappears upon
ng souuon because carbonyl C-atom (C-1) of each
glucose unit is involved in glycosidic linkaoe, On hudroela or enzymes, starch glves a mbxture of smaller chain
d
molecules called maltose and finally alves d-D-Guco
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 CeH1o0s)n (CeH1o0s)r C2H22011 CE CeH120s
Starch Maltose -D-Glucose
Starch is the major component of our food. In our body, it is digested by the enzyme amylase present in saliva. The end product of
starch hydrolysis is glucose which is the source of energy in our body.
Starch is a mixture of 15-20% amylose and 80-85% amylopectin both of which are polysaccharides of a-Glucose. Baoth of them
havelinkage between C-1 of one glucose unit and C-4 of the other. Differences belween them are
Amylose Amylopectin
01 Itis a linear polysaccharide. It is a branched chain polysaccharide.
02 water
tis soluble. t is w insolubl
03 It gives blue colour with lodine solution.
04 It has 200-1000 glucose units.
t does not give blue colour with lodine solution.
| thas hundreds of smal chains of 25-30 glucose units
02 CELLULOSE(CH0)
It is the most abundant organic material and the structural polysaccharide of higher plants which constitutes the cell wall. Wood
contains 45-5076 while cotton contains 90-95%% cellulose. Over 50% of the total organic matter in the living world is cellulose. It is a
colourless and amorphous solid which decomposes on heating. Cellulose is a linear polymer of B-D-Glucose which have C-C
gycosidic linkage between them. These chains are held together through multiple H-bonding to fom rigid bundles/fibers which acts
asa perfect material for building the cell wall.
Like starch, cellulose does not reduce Tollen's reagen/Fehling solution but unlike starch, tis not fermented by yeast. It is hydrolyzed
with diute sulphuric acid at high pressure to give p-Glucose. It is used in the manufacture of gun cotton (explosive), cellulose acetate
plastics,), methyl cellulose (cosmelics), rayon etc.
Cellulose is not digested by humans due to the lack of enzyme cellulase. Although. grazing animals also lack this enzyme but they
have cellulotic bacteria present in their stomach which secrete cellulase and help in the digestion of cellulose.
03 GLYCoGEN/ANIMAL STARCH

In animal body, carbohydrates are storad as glycogen. It is also called animal starch because its structure is similar to
amylopectin afthough more branched. It present in liver, muscles and brain. When the body needs glucose, enzymes break
itis is
0Own giycogen into glucOSe. Glycogen is also found in yeast and fungi.
Importance of Carbohydrates: Carbohydrates are essential for life in both plants and animals.
a
01 hey torm major porion of our food e.g., honey is used as an instant source of energy.
02 carbohydrates are used as storage molecules as starch in plants and glycogen in animals.
03 Cell wall of bacteria and plants is made up of cellulose.
04 Cellulose in the fom of wood is used to make fumiture and cotton fibre is used to make clothes.
05 carbohydrates provide raw materials for many importantindustries like textiles, paper, breweries etc.
06 Two aldopentoses namely D-ribose and 2-deoxyD-ibose are present in nucdeic acids.
07 Carbohydrates are found in biosystems in combination with many proteins and lipids.
AMINO ACIDs
These are the compounds which contain-NH2 as well as coOH groups. Depending on relative positions R-CH-COOH
of these groups in the molecule, amino acids may be classified into a, B, y . Deneral Tofmula o
s.
a-amino acds is given alongside in which-R may or may not contain other functional groups. NH2

Nomenclature of Amino Aclds :

Common names are based on a particular property or source of the amino acideg. glycine is named so because it is sweet in taste
(Greek:gykos means swee, tyrosine is named so because t was obtained from cheese (Greek: (yros means cheese). Amino acids
are mosty represented by three ietter symbois but sometimes one letter symbol is also used e.g.. Glycine (gly/G), Alanine (ala/A) etc.
:
Classification of Amino Aclds Depending on the relative number of -NHa and -COOH groups, amino acids are classifed as follows
:
A 01 Noutral Amino aclds In these amino aclds, number of -NHa and-coOH groups is same.
02 Acldic Amino aclds : in these amino acids, number of -coOH groups is more than the number of-NH groups
:
03 Basie Anmino acide In these amino acids, number of -NH groups is more than the number of -CoOH groupa
B Total 20 amino acids are known. Animals can synthesize 10of them which are called non-essential amino acids eg. gycine, serine
elc. Remaning have to be supplied in the tom of diet and are called essential amino acids e.g., valine, lysine etc. Lack of essential
amino acds causes disease Kwashionkar, MIK, egg and meat contain most of the amino acids. Com, rlce and wheat have low
ysine, typlophan and threonine oontent but protein rich pulses supplement them.
Physical Properties of Amino Acide:
hy are coloures, water soluble and hiph meting cryetalino solde becaue they behave ke R-CH-cooH R-CH-cOo =
sall raher than an amine or the carboxyllc acid. Due to the presence of NH2 as well as-coOH
Sroupco0H groupamino can loose a lon whille-NHa group can accept it In aqueous solution at
PHZ That
s why, acids exiat as dlpolar lonerwittor lons which are neutral but contain
DolUh positye and negalive charges
due to transfer of H' on within the molecule as shown
NHa NHs
zwitter lon
mino acids are amphotertc in nature because they act as R-H-COOH R-CH-COO R-CH-CO0H0
proton acoeptors in acidic medium and as prolon donors in
NHa "NHa NRa
basic medilum,
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 BIOMOLEcULES 05
Except Glycine (R=H), other naturally occurring amino acids are optically active because a-Carbon in them is the chiral center. They,
ll
therefore, exist in D and L configurations. Most of the naturally occuring amino acids are L-Amino acids (-NH2 on LHs). Proteins are
made up of L-amino acids only. Amino acids maintain nitrogen balance in the body.
PROTEINS
Proteins are high molecular weight polymers of a-amino acids present in all parts of the body. They form the fundamental basis of
structure and functions of life. Protoplasm of all plant and animal cells contain 10-20% proteins. Proteins are required for the growth and
maintenance of the body e.g., all enzymes (which catalyze biological processes), hormones (which regulate metabolic processes) and
antibodies (which protect the body against toxic substances) are proteins. Thus, we can say that proteins are extremely important
compounds [Greek proteios = of prime importance].
All proteins contain C. H, 0, N and S although some may contain P, and traces of metals like Fe, Cu, Zn and Mn. On hydrolysis, all
I
proteins give peptides of varying molecular masses which on complete hydrolysis give a-amino acids.
Proteins Peptides Amino acids
Classification of Proteins
Onthe basis of molecular shape, proteins are of two types:
01 Fibrous Proteins : They have fibre like structure formed by H-bonding or sulphide bonds between polypeptide chains which lie
paralel to each other. They are insoluble in water e.g., keratin (present in hair, wool, silk) and myosin (present in muscies), etc.
02 Globular Proteins : In these proteins, polypeptide chains are coiled which gives them a spherical shape. They are usually soluble
are
in water. Insulin and albumins common
the examples of globular proteins.
Structure of Proteins :
Proteins are the condensation polymers of amino acids in which amino acids are linked together by amide linkages called peptide bonds.
For the formation of a peptide bond, -coOH group of one and-NH2 group of the adjacent amino acid react together and lose a molecule
ofwater to fom a secondary amide group (-Co-NH-) Le., the peptide bond/peptide linkage as shown beloW
Peptide bond

H-N-CH-OH N-CH-f (Horizontal N-C-C-N-C-C.. chain is called

H backbone of polypeptide chain)
If R-H, amino acid is Glycine and if R=CHs, it is Alanine and the product of these two amino acids is a dipeptide called Glycylalanine [or
oup or ycne and-NH2 group ot Alanine have reacted together but if-NH2 group of Glycine
adcL A
andcooHgroup anin react togetherhena diterent produc is optained
than ten,
ten, then
ot
product is called a pooeid
the product is called a polypeptide.
then the
tO 10m , whih caledAlanyycne
Alaio nena
letrapeptide and so on. If the number of amino acids is
more

than
Structure and shape of proteins can be studied at four different levels, le., primary, secondary, teriary and quatemary. Each level is more
complex nan uie previous one.
01 Primary Structure of Proteins: A protein has one or more polypeptide chains. Sequence in which amino acids are aranged in
each chain is called its primary structure. This sequence is highly specific
for each protein which determines its function and biological
activity. Any change in this sequence can drastically change properties of protein e.g. in haemogiobin, 574 amino acid units arranged
in a specific order. Changing just one amino acid in the sequence makes itdefective which leads to the disease-sickle cell anaemia.
Normal Haemoglobin:-Val- His- Leu- Thr-Pro- Glu-Defective Haemoglobln Val- His-Leu-Thr-Thr-Glu- :-
Amino acid sequence in the protein Insulln was first determined by Dr. Fredric Sanger in 1953. Complete amino acid sequence of
several hundred proteins is now known.
02 Secondary Structure of Proteins: It refers fo the shape of polypeptide chains which arises due to regular folding of the backbone
or polypepude cnain.Derent pans or ne
ComOn Ypes of secondary re edogeby X-Rayyrogen
Cn confirmed
structures of proteins en
studies are bonong Deween o co andand -NH-groups.
-Ngroups. Two
Iwo

In this structure, backbone of polypeptide chain is twisted to form a helix. This twisting pattern is like right
aa-Helix structure
handed screw and is caled a-helix lLe., the chain is held verticaly and viewed from the top. it spirals clockwise from top to
f
bottom. Different parts of the same chain are held together by Intramolecular H-Bonding. Each tum of helie has approx 3.6
amino acids so that H-bonds are formed between CO group of 1"& NH group of 4 amino acid on adjacent tum of the helix.
b -Pleated/B-Sheet structure: In this type of protein structure, peptide chains are strelched out to the maximum in a zigzag
manner with the 'R groups of altemate amino acids on the same side. Nelghbouring chains are held together through
Intermolecular Hydrogen Bonding leading to the formatlon of flat sheet type structures. These sheets lie one above the other
Ikefolded pages of a book. Ihis gives rise to 3D-structure called -pleated sheet structure.
c Tertiary Structuro of Protelns: This structure arises due to overall folding and twisting of the secondary structures of
polypeptde chalns. 1his loding is dueto the interaclion between side chain groups which are held together through H-Bonding
van der Waal forces, disupnide linkages, hydrophoblc Interactlons etc. Itgives rise to two main molecular shapes to proteins
which are nbrous protoine (o9., Keralin, myosin) and globular protoins (e.9, insulin, albumins).
dQuatemary structure of proteins Some prolelns are made up of 2 or more polypeptide chalins which are called sub-units.
3D arrangement of these sub-units with respect to each other is known as quatemary structure.
Denaturation of Proteins
At nomal pH and temperature, aach proteln has a unlque 3D structure which le energetcaly most stable and it is blologlcally active. This
caled or the natve state of protein. fthe proten ls subjeted to a physicalor chemical treatment like change in pH, temperature, presence
ofsals other chemicals, may lose ts bologlcal
t t
activity because loses lts hgher structures (secondary, tertiary and quatemary)
wu aecng the primary etructure. This is egg
precptlates out from the solutlon e.g, coagulation of
a
called denaturatlon of proteln during which t uncolls Into random shape and
white on bolling and curdling of milk are the examples of denaturation of proteins.
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Functions of Proteins: Some of the biological functions of proteins are:
01 They serve as structural materials for animal tissues e g., keratin (skin, nails, feathers etc), myosin (muscle).
02 They transport cellular necessities like oxygen, metals, fatty acids etc eg., haemoglobin acts as oxygen carrier
03 Some proteins act as enzymes which are biocatalysts.
04 Some proteins regulate metabolic processes e.g, insulin in pancreas maintains blood sugar level and thyroglobulin in thyroid
glands heps in syntthesis of the homonehyroxine.
05 | Some proteins called antibodies, fight against infectious species like virus and bacteria.
ENZY
Many complex biochemical reactions take place in a living cell at very fast speeds even under mild conditions of body temperature and
pH. Outside the living cell, these reactions would proceed very slowly due to the absence of certain biocatalysts called enzymes which
are present in living ceils e.g.. it would take us 50 years to digest one meal in the absence of these catalysts. Enzymes lead to proper
degradation of constituents of food into simpler molecules which can be easily absorbed by the body. Enzymes are synthesized in living
systems and they regulate many biological activities.
Almost all enzymes are globular proteins. They are highly specific for a particular reaction. They are generally named after the
compound or class of compounds on which they work and their names end with the sutfix -ase e9, the enzyme that catalyses hydrolysis
of maltose into glucose is named as maltase. Sometmes they are also named after the reaction where they are used eg. the enzymes
which catalyze oxidation of one substrate with simultaneous reduction of another substrate are named as oxidoreductase enzymes.
a
Since there are large number of biological reactions taking place in the body and each reaction is catalyzed by a specific enzyme,
number of enzymes functioning in a living system is very large. On an average, a living cell has 3000 different enzymes each cataiyzing
a different reaction. Out of these, only about 300 (10%) are commercially available.
Properties ot Enzymes
01 They can catalyze the reaction upto ten million times.
02 They are highly spocific in their action ie, each enzyme catalyzes a specific reaction only.
03 They are active at moderate body temperature and pH only.
04 Their action is inhibited by some organic and inorganic molecules called enzyme inhibitors
05 Yields in enzyme catalyzed reactions are quantitative.
06 Most of the enzyme catalyzed reactions are reversible and same enzyme catalyzes reaction in both the directions.
Enzymes are colloidal in nature. They are required in very small quantity because an enzyme molecule may be regenerated millions of
timesin one minute. Ahougn enymes are regenerated during the reaction but sometimes they becomes inactivate dunng the reacton
Gueto which they have to De constanty repiaced by synthesis in the body.
Specificity and Mochanism of Enzyme Catalyzed Reactions:
a biochemical reaction by providing an alternatve pathway for the reaction whose energy of activation is lower.
An enzyme catalyzes
Steps invoved in enzyme catalyzed reactons are given below
Adsorption of substrate (S) on the surface of enzyme (E to form a complex E+S ES
A reaction leading to the formation of products on the surface of the enzyme :
ES] (EP_
Release of products from enzyme-products complex to regenerate the enzyme -
i | [EP] EP
There are certain active sites on the surface of enzyme where substrate molecules bind themseves. These active sites are so shaped
that only a specihic substrate can into This accounts for the high degree of speciicity of enzymes.
t t.
Step-@
Sep-0

Products

Appllcations of Enymes
01 In cheese production. 02 In food industry for the production of sweet syrups from com starch.
enzymes are
03 Several used in fermentation for the manufacture of wine and beer.
Enzymes and Diseases:
01 Congenital (by birth) disease Phenylketone uroa ls due tothe deficlency of the enzyme Phenylalanine hydroxylase. This results
n accumulalon of compounds in the body leading to brain damage and mental retardation in children. This disease can be prevented
by a diet ith low Phenylalanine content.
02 Alblnism is caused by the deficlency of Tyroslnaso, lts symptoms are lack of plgmentation of skin, hair and retina.
03 a
Enzyme Streptokinaso is used to disaolve blood clota in coronary artery and thus provent heart attack.
VITAMINS
These are organlc compounds other than fats, proteins, carbohydrates etc whlch are required In small amounts and are necessary to
maintain noma and orown oranima. ney are notyntheszed oy animais and have to be supplied in the dilet Pants
can synthesize al hean
vitamins but animais cannot. 5acterna present in the gut can aynthesze tew of them. Neither are they used in building
celle nor 85 a source of energy. Uhey act as catalysta in some DIo10glcal processes. Their deficiency causes serious diseases.
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 BIOMOLECULES
07
Chemically, they belong to different classes but for simplicity, they are represented as Vitamin A, B, C, D, E, K, etc. On the basis of their
solubility,they are cdlassifed into two categones
01 Water soluble vitamins: Vitamins B and C are soluble in water. They should be regularly supplied in the diet because they are
readily excreted in urine and therefore cannot be stored in our body (except B12).
02 Oll soluble vitamins: They are soluble in oils and fats but insoluble in water e.9, A, D, E, and K. They are stored in liver and
0pose tissues.
Vitamins and Diseases:
SN Vitamin Sources Diseases
01 Vit-A/Retinol Fish liver oil, carrots, butter and milk Xerophthalmia (hardening of conea of eyes), night
Dlindness, Stunted growth and drying of skin
02 Vit-B (Thiamine) Yeast, milk, green vegetabies and cereals Beri-Beri (loss of apetite, retarded growth)
03 Vit-B2 (Ribofavin) Milk, eggwhite, liver, kidney Chellosis (issuring at corners of mouth and lips), digestive
and skin disorders
04 Vit-Be (Pyridoxine) Yeast, milk, egg yolk, cereals and grams Convulsions
05 Vit-Bi2 Meat, fish, egg and curd Pernicious anaemia (RBC deficiency in haemoglobin)
06 Vit-CIAscorbic acid citrus fruits and green vegetables Anemia, scurvy (bleeding gums), dental caries (decay of
eetn) ana pyorrnea L
07 Vit-D Exposure to sunlight, fish and egg yolk Rickets-a disease related to bones
Vit-E Vegetable oils Increased fragility of RBC's and muscular weakness
9 Vit-K Green leary vegetables Increases blood clotting time
Vit-8Complex:
tis agreen of
group vitamin
lke Bi, Ba. Ba, Be. Br2, Biotin, Pantothenic acid, Folic acid and Nicotinic acid. They occur together
in milk, liver, cereals, lealy vegetables, yeast, egg elc.
NUCLEIC ACIDS
Nuclelc acids are high molecular weight compounds present in all iving cells. They are present in chromosomes of cell nuclel and also
in the cytoplasm. They are called nucleic acids because the first nucleic acid was isolated from the nucleus of a puss cell and was found
tobe acidic in nature, Nuceic acids are present in association with certain proteins called nucleoproteins. Two main functions of Nucleic
acids are
01 Proteins synthesis (inciuding enzymes)
02 | Transfer of genetic information ile., hereditary characteristics from generation to generation.
Nucleic acids are of two types: 01 Deoxyribo Nucleic acids (DNA) 02 Ribo Nucleic acids (RNA).
Structures of Nuclelc Aclds:_
Nucleic acids are the biopolymer whose monomeric units are nucleotides. That is why, nuclelc acids are also called polynucleotides.
Each nudeotde is in tum made up of following three components
01 A Pentose sugar which is p-D-Ribose in RNA and B-0-2-Deoxyribose in DNA.
02 A Phosrhoric acid unit.
03ANirogen containing Heterocyclle Base. This base is a Purine or Pyrimidine detvative. Bases derived from purine are Adanine
anannewereas those denved from pyrimidine are ytosine (G). Thymine (T) and Uracil (U). Nucleotides of DNA
haveA, G, C and T but not U whereas nucleotides of RNA have A, G, C and U but not T.
A nitrogenousbase and a Pentose sugar combine to form a Nucleoside. Depending on the sugar present, nucleosides are of two types

eold nonrbonucleosides. One of the -OH groups of sugar in the nucleoslde foms an ester witrh phosphoric
which becomes a Nucleotude. hus,
acid
SugarBase Nucleoside
Nucleoside Phosphoric acid Nucleotide
Depending on ne sugar present, nucieotides are of 2 types Ribonucleotides Deoxyribonucleotides.
DNA consists of two polynucleotide strands coled around each other in the form of a
double helix. Backbone of each strand is made up of nucleosides connected t
from this hackhn
UOUgn Pnospnate ester bonds in such a manner that the bases extend
shown
DNA has two such strands which are held together through -bonding
bebween bases of wo strands. This H-Bonding is hlghly specifo In whlch A
on one strand is H-bonded to T on the other strand through two H-bonds while
Gonone strand is H-bonded to C on the other strand through three H-bonds
as shown Deiow
Due to highly specific base palring, two strands of DNA are complemontary to each other because
base sequence on one strand
auiomaucaly detemines the base sequence on the other strand.
In secondary structure of RNA, hellces are only slngle stranded. Sometlmes they fold back on themselves to fom a double helix
structure. RNA molecules are of three types
and they perform different functions. They are named as mossenger RNA (M-RNA).
ribosomal RNA (r-RNA) and transfer RNA (t-RNA).
Strucure of RNA ls almost similar to tho structure of DNA, Somo etructural and functional diferences between DNA and RNA are
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 BiOMOLECULES D8
DNA RNA

01
02
Sugar present is 2-Deoxyribose.
Pyrimidine bases present are C andT,
Sugar present is Ribose.
Pyrimidine bases present are C and
.
03 Double stranded structure Single stranded structure.
Mainly ocCurs in cytoplasm of the cell.
04 Mainly ocurs in the nucleus of the cell.
05 1t replicates. I does not replicate.
It controls the synthesis of proteins.
O6 It controls transmission of hereditary characteristics.
Molecular weight is 20,000-40,000.
07 Molecular weight is 6-16 milion.
Biological Functions of Nucleic Acids:
:
01 Transmission of Hereditary Characteristics DNA is the chemical basis of heredity and genelic information It is respona ble for
maintaining the identity of diferent species of organisms over milions of years. DNA molecule capable of self duplication
A is during
cell division and identical DNA strands are transfered to daugnter cells.
RNA
02 Protoins Synthesis: Another important function of nucleic acids is synthesis of proteins. Proteins are synthesized by various
molecules in the cell but the message 1or the synthesis of a particular protein is present in DNA.

INTEXT QUESTIONS OF NCERT WITH ANSWERS

o1 Glucose and sucrose are soluble in water but cyclohexane and benzene are insoluble in water. Explan.
Glucose and sucrose are polar compounds and therefore soluble in water but cyclohexane and benzene are non-polar compounds
and therefore they are insoluble in water.
are and p-D-Galactose.
02 What are the expected producds of hydrolysis of lactose ? Hydrolysis products of lactose -D-Glucose
03 How do you explain the absence of aldehyde group in the pentaacetate of D-glucose ?
Pentaacetate of D-glucose does not react with bhydroxylamine which shows the absence of aldehyde group in
04 MP's and solubility in water of amino acids are generally higher than that of the corresponding halo acids, Explain
Amino acids exist as zwiter ions and thus behave like ionic compds. That is wthy, they have high MP's and are soluble in water.
05 Where does the water present in the eg9 go after boiling the egg ?
When egg is boled, water present init is used up denaturation of proteins through H-bonding
06 Why cannot vitamin-C be stored in our bocdy 7
Vitamin-C is soluble in water and readly excreted in urine. That is why, it cannot be stored in our body:
07 What products would be formed when a nucleotide from DNA containing thymine is hydrolysed
:
Products of tydrolysis of a nuclotide from DNA are p-D-2-Deoxyibose, phosphoric acid and basesA, T, G &C.
08 When RNA Is hydrolysed, there is no relationship among the quantities of diferent bases obtained. VWhat does this facd suggest
about the structure of RNA 7
This suggests that RNA has single stranded structure.
EXERCISE QUESTIONS OF NCERT WITH ANSWERS
01 What are monosaccharides ? These are the carbohydrates which do not get hydrolyze e.g. glucose.
02 What are reducing sugars
These are the carbohydrates which have free carbonyl group and can reduce Tollen's reagentUFehling solurtion
03 Wnite two main functions of carbohydrates in plants.
Two main functions of carbohydrates are : (0) to support plant structure (oellulose)| () to store chemical energy (sugar & starch)
:
04 Classify following into monosaccharides and disaccharides Ribose, 2-deaxyribose, maltose, galactose, fructose and lactose._
Monosaccharides: Ribose, 2-deoxyribose, galactose and fructose :
Dlsaccharides Maltose and lactose.
gycogen How It
05 What is ? is diferent from starch ?
It ls a branched polysacchalde present in animals which acts as food reserve. It is present in liver, muscles and brain. When the
body needs glucose, enzymes break down glycogen Into glucose. On the other hand, starch Is a polymer of a-Glucose which has
wo components amylase and amylopectin.
What do you understand by the term oycosidic linkage ?
Oxide linkege (-0-) formed by condensation of two monosaccharide units is called the glucosidl linkage

07 What are the hydrolysis products of () sucrose and () lactose ?

0) Sucroses a-D-(t)-Glucose & p-D-t>Fructose
() Lactoses4-D-Galactose & p-D-Glucose
08 What is the basic structural diference between starch and cellulose?
Starch ls a miature of linear & branchod polymer of a-D-Glucose whilo celluloso is a linear poymer of 9-D-Glucose
09 What happens when D-glucose is troated with the following reagents ? HI Bromine water (lU) HNO» ?
() ()
When treated with () H, plucose Is reduces to n-Hexane () Bromine water, glucose is oxidised to gluconic acld and (1) HNOs
9lucose is Oxidised to saccharlc acld
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 BIOMOLECULES

10 Enumerate the reactions of D-glucose which cannot be explained by its open chain structure.
Open chain structure of glucose does not explain following reactions/observations
1. Although it has an aldehydic group but t does not give 2,4-DNPH test and il does not form addition product with NaHSOs.
2. Glucose pentaacetate does not react with hydroxylamine indicating the absence of free-CHO group.
3.ExIstence of its two foms called a-GlucOse and f-Glucose 4. Mutarotation in glucose
11 What are essential and non-essential amino acids 7 Give two examples of each type
Out of 20 amino acids known,animalsand can synthesize 10 which are called non-essential amino acids e.g. glycine and serine. Rest
to
have be supplied in fom ofdiet are called essential amino acids e.g. valine and lysine
the
12 Define the following as related to proteins (0) Peptide linkage Primary structure Denaturation. See pages 5 and 6
() (i)
13 What are the common types of secondary structure of proteins
?
:
common types of secondany structure of proteins are (1) a-Helix siructure (2) B-Pleated/ß-Sheet structure
14 What type of bonding helps in stabilising the a-helix structure of proteins ?
ntramolecular hydrogen bonding helps in stabilising the a-helix structure of proteins.
15Differentiate between globular and fibrous proteins. [Ans
Fibrous Proteina olypeptide chain le parallel and are held together by bhydrogen bonding and disulphide bonda, then fibre
nk sthicures formed. Such proteins aregeneraly insoluble in water. (b)Globular Proteins : In these proteins, polypeptide chains
are coecd wnicn gives nem a spherical shape. They are usually soluble in water
16 HOW do you explain the amphoteric behaviour of amino acids ?
hey are amphoteric in nature because they act as proton acceptors in acidicmedium and proton donors in basic medium.
R-CH-COOH R-CH-COO R-CH-Coo H:0o

NH NH3 NH2
natare enzymes 7Enzymes are biological catalysts present in living systems. Chemically they are proteins.
18 What is the effect of denaturation on the structure of proteins ?
On denaturation, proteins uncoil into a random shape and ppt out from the solution. They lose their secondary, tertiary quaternary
and
structures without affectung the primary structure.
19 How are vitamins classifed ? Name the vitamin responsible for the coagulation of blood.
For classification, see page-7. Vitamin-K leads to blood clotting.
20 Why are vitamin-A and vitamin-C essential to us ?
Vitamin-A: Because its deficiency causes night blindness, stunted growth and drying of skin etc. Vitamin-c : Because its deficiency
Causes anemia, scuirvy (bleeding gums), dental caries (decay of teeth) and pyorhea.
21 What are nucleic acids 7 Mention their two important functions.
Nucleic acids are high molecular weight compounds present in chromosomes cell nuclei and also in the cytoplasm.
of Their twoo
important functions are (0) Proteln synthesis () Replication I.e. transmission of heredity
a
22 What is the difference between a nucleoside and nucleotide ?
A nucleoside is made up of a nitrogenous base and a pentose sugar while a nucleotide is made up of a nitrogenous
base, a pentose
5Ugarand a phosphonc acid unit.
23 The two strands in DNA are not identical but are complementary. Explain.
H-Bonding between nitrogenous bases of ftwo strands highly specific. A on one strand is H-bonded to T on
wo H-bonds whereas G on one strand is H-bonded toisCon the other strand through the other strand through
three H-bonds. Due to this, base sequence on
one suanO Buiomaucaly oetetnines Dase Sequence on ne ouner surand 1.e, ney are compiementary to
each other but not Identical
24 Write the important structural and functional differences between DNA and RNA. See page-08
25 What are the diferent types of RNA found in the cell ?
| Different types of RNA are messenger RNA (M-RNA), ribosomal RNA (-RNA) and transfer RNA (-RNA).
sOME EXTRA QUESTIONS BASED ON THIS CHAPTER
01 Deline carbohydrates. on what basis are they cassified into mono, d- and polysaccharides Give examples.
?
02 How are monosaccharides classified on the basis of number of carbon atoms ? Give examples.
03 Optical rotation of a- and Glucose are 111 and 19.2 respectively but optical rotaton an aqueous
of solution of either of the two
m6 1e, D2.5, Wny 7 OR What happens when a- or B-Glucose is dissolved in water ?
04 Name the polysaccharides which constitute starch. Give differences In thelr properties.
05 How are carbohydrates classifed into reduUcing and non-reducing carbohydrates/6Ugars
06 What does the formation of following products from glucose Indilcate about the structure
of glucose?
(a) Glucose yanohydrin (b) Gluconic acld (C) dlucose pentaacetate (d) Hexane
07 Sucose is dextro-rotatory but mixture of lts hydrolysls products ls laevo-rotatory, why ? OR Write a short note on inverslon of sugar.
08 Why is glucose given to patients under exhaustion ?
Because glucose in blood Is the main source of enerOy for the cells of brain
and nervous system.
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 BIOMOLECULES 10

09 are
What the monosaccharides oblained by hydrolysis of
the canesugar, maltose and lactose ?
10 Where does excess of glucose in our body go ? Ans: It is stored in liver as gtycogen which is broken by cells when required
11 Carbohydrates are hydrates of carbon' Giving examples, justfy why this definition was initialy used and what are its limitations
12 Why are the cyclic structures of glucose and fructose called Pyranose structure and Furanose structure respectvely
13 How do we assign 'D' or L' configuration to a (a) carbohydrate (b) amino acid 7
14 What are amino acids ? How many naturally occuring amino acids are known
15 On what basis are amino acids classified into neutral, acidic and basic amino acids?
16| What are essential and non-essential amino acids ? Give two examples of each type.
you prove thata neutral amino acid is ampholeric in nature ?
17Howwill
are
18 Why the melting points of amino acids higher than that of corresponding halo acids ?
19 On electrolysis in acidic medium, amino acids go towards cathode whereas in akaline medum, they go towards anode, winy
20 How may tripeptides containing glycine, alanine and phenylalanine are possible 7 Give their threeletter abbreviations.
Total 6 tripeptides are possible as given below: (a) Giy-Ala-Phe (b) Gly-Phe-Ala () Ala-Gly-Phe
(d) Ala-Phe-Gly (c) Phe-Gly-Ala (f) Phe-Ala-Gly
you structure of proteins or globular proteins 7
by
21 What do you understand tertiary or
22 What do understand by B-sheet B-pleated structure of proteins?
23 How many amino acids are there in one helix of the protein and how is the helix stabilized 7
24 Tertiary structure of proteins is disrupted in an aqueous solution above 80 C but primary structure is not, explain.
25 At high temperature. proteins get denatured in which they Iose their native state and get uncoiled i.e., they lose their sec, tertiary and
quatemary structures but peptide bonds remain intact so that their primary structure is retained.
What are the causes of following diseases: (a) Kwashiorkar (b) Sickel cell anaemia (¢) Pheny! ketone urea (O) Albinism
26 Why are nucleic acids named so ? Why are they also called nucleoproteins ?
a
27 What is the difference betweena nucleotide and nucleoside 7
28 How many H-bonds are present between bases of opposite strands in DNA ?_
t
29 In DNA, ATIGC ratio is 0.8. If has 4,20,000 molecules of G, calculate the number of T molecules it has. Ans:3,36,000
30 What are the products obtained on complete hydrolysis of (a) DNA (6) RNA ?
31 Unlike DNA, there is no relationship among the quantities of four amino acids obtained upon hydrolysis of RNA. What does this
ndicate about the structure of RNA ?
32 What do you understand by the statement, Two strands of DNA are complimentary to each other 7
:
33 What is the disease caused by the deficiency of follwing vitamins (@)B1 (b) B2 (c) Bo (d) Br2 (e)D (0 C.
34 Ghve the base sequence on the strand which is complimentary to the DNA fragment: TAACGACG.| 35 What is glycogen ?
36 What do you understand by denaturation of proteins 7 Write a short note on bonding in proteins.
37
38 What do you understand by secondary structure of proteins?39What do you understand by primary structure of proteins 7
40 Why cellulose act as a perfect building material for cell walls? Amino acids of which configuration are present in proteins ?
41
-Glucose.43 Give wo important products of cellulose and give their uses.
42 Give any four differences between a-Glucose and non-sugars
44 How are carbohydrates classified into sugars and ? 45 How many amino acid units are there in haemoglobin ?
you Why is cellulose not nourishing for human beings ?
46 What do understand by native structure ofa protein ? 47
48 Name the vitamins which is responsible for blood clotüing.
49 In D-(+-Glucose, what do "'D' and (t) stand for ?
50 How is glucose prepared from cane sugar ans starch 51 Give one major tunction each of starch and cellulose.
52 Sucrose is a reducing or non-reducing sugar and why ?
53 Give diferences between Amylose and Amylopectin.
64 How do gazing animals digest cellulose 7 55 Give main functlons of: (a) proteins (b) insulin.
56 What are the constituent units of cellulose ? S7What are anomers Explaln with reference to glucose.
?
are
58 What biomolecules 7 69Why aro carbohydrates also called saccharides ?
60 Name the only optically Inactive amino acld, 61 What are aldoses and ketoses ? Gve examples.
62 What do you understand by mutarotation ? 63 a
In what form does neutral amino acid exist ? Drawit.
64 Give the function of amino acids, 65Give steps Involved in enzyme catalyzed reactions.
66Amino acids are amphoteric in nature, why 7 an important use of the enzyme- streptokinase.
are enzymes
67Gve
68 What ?What is thelr function 7 69 Give differences between DNA and RNA.
70 Write a short note on specificlty of enzymes.
71 What are the diferent types of RNA present in the cell ?
72 What is the monomer of nucleic acids called ? 73 What are vitamins ? What is their role in our body ?
74 Give two important functions of nucleic aclds | 75 What is the use of cellulose in human dlet ?
Ans-76: Although cellulose not digested by humans and thus not nourishing for humans, but it provides necessary roughage for
ls
proper uncuoning of Uhe large intesune.
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