Bio Molecules
Bio Molecules
4 Insulin production of its action in human body are (a) I, II and III (b) II and III
responsible for the level of diabetes. This compound (c) I and II (d) Only III
belongs to which of the following categories? 11 Identify the correct statement regarding enzymes.
(a) A coenzyme (b) A hormone (a) Enzymes are specific biological catalysts that can
(c) An enzyme (d) An antibiotic normally function at very high temperatures (T ~ 100 K)
5 RNA and DNA are chiral molecules, their chirality is (b) Enzymes are normally heterogeneous catalysts that are
due to very specific in their action
(a) L-sugar component (c) Enzymes are specific biological catalysts that cannot be
(b) chiral bases poisoned
(c) D-sugar component (d) Enzymes are specific biological catalysts that possess
(d) chiral phosphate ester units well defined active sites
6 In an amino acid, the carboxyl group ionises at 12 In an electric field, if an amino acid migrate towards
pKa1 = 2.34 and ammonium ion at pKa2 = 9.6. The cathode, the pH of the solution is said to be
isolectric point of the amino acid is at pH (a) less than pI (b) more than pI
(a) 5.97 (b) 2.34 (c) 9.60 (d) 6.97 (c) equal to pI (d) 7
7 The enzyme which facilitates internal rearrangement in 13 The correct statement in respect of protein haemoglobin
3-phosphoglyceric acid to form 2-phosphoglyceric acid is is that it
(a) aldolase (a) acts as an oxygen carrier in the blood
(b) triose phosphate isomerase (b) forms antibodies and offers resistance to diseases
(c) phosphoglycero mutase (c) functions as a catalyst for biological reactions
(d) pyruvate kinase (d) maintains blood sugar level
14 Which statement is incorrect about peptide bond (c) C—N bond length in proteins is smaller than usual bond
O length of C—N bond
• • (d) None of the above
C N H ?
15 The α-D glucose and β-D-glucose differ from each other
(a) C—N bond length in proteins is longer than usual bond due to difference in carbon with respect to its
length of C—N bond
(a) conformation (b) configuration
(b) Spectroscopic analysis show planar structure of
(c) number of —OH groups (d) size of hemiacetal ring
C NH group
O
ANSWERS
SESSION 1 1 (c) 2 (a) 3 (d) 4 (c) 5 (d) 6 (a) 7 (d) 8 (b) 9 (c) 10 (d)
11 (b) 12 (a) 13 (a) 14 (c) 15 (c) 16 (b) 17 (c) 18 (b) 19 (a) 20 (d)
21 (b) 22 (d) 23 (d) 24 (c) 25 (b) 26 (c) 27 (b) 28 (c) 29 (c) 30 (a)
SESSION 2 1 (a) 2 (a) 3 (d) 4 (b) 5 (c) 6 (a) 7 (c) 8 (c) 9 (c) 10 (a)
11 (d) 12 (a) 13 (a) 14 (c) 15 (b)
Here, the configuration of sucrose changes (gets inverted) after 21 Disulphide bond may be reduced to thiol by means of reagents,
hydrolysis, thus its hydrolysis is called inversion. i.e. NaBH4 , which shows the presence of thiol group in
disulphide bond formation.
13 α-keratin is water insoluble fibrous protein. It is the major
constituent of nail, hair and skin. 22 Conjugated proteins on hydrolysis give a non-protein portion
14 Cellulose is a polysaccharide, composed of D-glucose units alongwith α-amino acid. The non-protein portion is called
which are joined by β -glycosidic linkages. prosthetic group.
H+
(C 6H10O 5 )n + nH2O → nC 6H12O 6 Protein Prosthetic group
Cellulose D -glucose
Phosphoprotein Lipid (e.g. lecithin)
15 Starch contains two components amylose and amylopectin. Glycoprotein Sugar
Chemically, amylose is a long unbranched chain with 200-1000 Chromoprotein Coloured matter such as
α-D- (+ )-glucose units held by C1-C 4 glycosidic linkage. red coloured protophyrin
Amylopectin is a branched chain polymer of α -D-glucose
units in which chain is formed by C1-C 4 glycosidic linkage Since, all of them have non-protein part hence, all of them are
where branching occurs by C1-C 6 glycosidic linkage. conjugated proteins.
23 Denaturation of protein occur when it is subjected to physical 3 Proteins gives blue voilet colour with ninhydrin while
change like change in temperature or chemical change like carbohydrate gives negative test with ninhydrin. Carbohydrates
change in pH, the hydrogen bonds are disturbed. As a result, give brown red precipitate with benedict’s solution. Hence,
globules unfolds and helix get uncoiled so that protein losses its compound is monosaccharide.
biological activity. Hence, the denaturation of protein makes the 4 Insulin is a proteinaceous hormone. It is secreted by pancreas
protein inactive is not correct. and controls the metabolism of glucose and maintains glucose
24 Vitamin B12 contains cobalt and its chemical name is level in the blood.
cyanocobalamin. Its deficiency causes pernicious anaemia. 5 RNA and DNA molecules have ribose and deoxyribose sugar
25 Vitramin C is also known as ascorbic acid. respectively. Both are chiral, their chirality is due to D-ribose or
deoxyribose sugar component.
26 Epinephrine (adrenaline) hormone produced, the adrenal
2.34 + 9.6
medulla that helps the body to respond to emergency situations. 6 pH (at isoelectric point) = = 5.97
This stimulates glycogenolysis in the liver of human beings. 2
27 Deficiency of vitamin B1 causes beri-beri, which causes loss of 7 The internal rearrangement of 3-phosphoglyceric acid into
2-phospho glyceric acid takes place in the presence of enzyme
appetite and vigour, weak heart beat etc.
phosphoglyceromutase.
28 The pyrimidine bases present in DNA are cytosine and thymine 4HIO
while adenine and guanine are purine bases. 8 CH2 CH CH CH CH COOH →
4
HCHO
29 In RNA, uracil is present instead of thymine. OH OH OH OH OH
Gluconic acid + 3HCOOH + C HCOOH
30 In DNA, the two strands are held together by hydrogen bonds.
For example guanine is bonded to cytosine and adenine to 9 Glucose is present in pyranose form. O
thynine by hydrogen bonding. 10 In all the three structures (I, II and III), the configuration of OH at
C-1 is towards right and hence, all have D-configuration.
SESSION 2 11 Enzymes have well defined active sites and their action are
1 Synthesis of RNA/DNA from phosphoric acid, ribose and specific in nature. They are called biological catalysts and work
cytosine is given below : at optimum temperature between 25 to 40°C.
Dehydration 12 Cations move towards cathode and when pH < pI, thus cationic
NH2
form dominates.
OH 5 4
3N
5
O
13 Haemoglobin act as an oxygen carrier in the blood because four
O P—OH HOCH2 OH 1 2
6
N Fe 2+ ions of haemoglobin can bind with 4 molecules of O 2 and
4 1
O
OH from oxyhaemoglobin.
H H H
H H Hb + O 2 → Oxyhaemoglobin
3 NH2
2
14 Peptide bond is formed by the reaction of COOH group of one
OH OH 5 4
3N amino acid with the NH2 group of another amino acid and
6 2 represented as
OH 1 _
O O O
–2H2O 5'
O P—O— CH2 O N +
4' 1' —C—NH— —C —NH—
OH
H
H H As partial double bond character found betweenC N bond, the
H
3' bond length of C N in protein should be smaller than usual
2'
C N bond.
OH OH
15 The isomer having the hydroxyl group ( OH) on the right is
Thus, ester linkages are at C 5 ′ and C1 ′ of sugar molecule. called α-D-glucose and one having the hydroxyl group ( OH)
2 Ring A is pyranose (6 membered ring containing one O-atom) on the left is called β-D-glucose. Such pairs of optical isomers
with α-glycosidic linkage and ring II is furanose with β -glycosidic which differ in the configuration only around C1 atom are called
linkage. anomers. Thus α-D-glucose and β-D-glucose are anomers.