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concise
BIOCHEMISTRY
MCQs
Aditya Arya | N K Sharma

First Edition
Concise Biochemistry
MCQs
Concise Biochemistry
MCQs
1st Edition

Dr. Digitally signed by Dr. Aditya

Arya
DN: cn=Dr. Aditya Arya, c=IN,
o=Drawing Pin Publishing,

Aditya ou=DPP,
email=drawingpinpublishing@g
mail.com
Reason: Dr Arya is the original

Arya Author of this book

Date: 2018.01.23 15:04:02
+05'30'

Aditya Arya, PhD

Defence Research and Development Organization
New Delhi, India
Narendra Kumar Sharma, PhD
Guangzhou Institute of Biomedicine and Health, China
New Delhi, India

CONCISE BIOCHEMISTRY MCQs, 1st Edition

ISBN 000-0-0000-0000-0
Copyright © 2017. Drawing Pin Publishing.

All rights reserved. No part of this publication may be reproduced

or transmitted in any form or by any means, electronic or
mechanical, including photocopying, recording, or any other
storage and retrieval system, without prior written permission
of the publisher. All the copyright related queries may be
directly sent to the publisher at drawingpinbooks@gmail.com

Disclaimer
Although, utmost care has been taken to avoid any errors
in the preparation of answers keys, however in case of any
discrepancies or loss of any kind due to incorrect answers or
solutions, authors or publishers shall not be responsible. The
names ‘Chintukla’, ‘Champakali’ and ‘Champaklal’ used in the
questions are imaginary characters to enhance the learning
experience and bear no resemblance with any person. Also,
the concepts of biochemistry mentioned in the book are not for
clinical advice or suggestions.

Cover Design: Dr. Aditya Arya

A part of structure of human serum albumin protein, originally
submitted to RCSB by Sugio, S. et al.

Typesetting Editor: Mr. Rakesh

Production Manager: Shashank Arya
Copyediting: Subhojit Paul
Printed in India
To Anjali
 Preface
Concise Biochemistry MCQs is an outcome of the tremendous success of the previous theory book Concise Biochemistry:
Fundamental Principles, 2nd edition. Considering the suggestions of the students and readers, a large collection
of multiple choice questions was prepared including about twenty percent of questions from nationwide entrance
examinations for MSc and Ph.D. The book will not only complement the theory book but also provide a comprehensive
understanding and routine practice in biochemistry. This book contains more than 2000 questions, based on different
facets of biochemistry. The distribution of chapters and topics has been retained similar to the theory book. There are
three sections, first includes essential chemistry for biologists, second detailed description of all biomolecules and
third included metabolism and enzymology. Unlike most of the other MCQ books, this book is not a random collection
of questions, but also provides a detailed solution to a large number of questions as well. Additionally, each chapter
begins with the review of basic concepts pertaining to the various topic which is a crisp summary of the detailed chapter
in the theory book. This is followed by the important useful information such as commonly used formulae, information
on biomolecules, enzyme regulation priming the readers for solving questions. Various levels of difficulty have been
considered in preparing the MCQs that includes memory based questions, reasoning based questions and analytical
questions. Some chapters such as amino acids, and metabolism which have more diversity in topics, the number of
questions have been increased beyond the 100 MCQs per chapter. A small crossword puzzle is included in each chapter
to relax and revise the chapter. At the end of each section, two small test papers for practice are included, paper two
has higher difficulty level than paper one. Answers to puzzle and test solution may be found on the website of the
publisher.
I must acknowledge the efforts of several other people who supported in writing this book. Initially, I would extend
my sincere acknowledgment to my Biochemistry teachers Dr. CK Shrotri and Prof. GS Selvam, who introduced me this
subject at undergraduate and postgraduate level respectively. Efforts put forward by Ms. Jayanti Jha and Ms. Neha
Chauhan in preparing the key for few questions and proofreading are deeply acknowledged. I also acknowledge the
efforts and inputs made by my colleagues Anamika Gangwar, Shikha Jain, Subhojit Paul, Amit Kumar, Nassruddin and
many other students who have contributed their ideas. My grandfather, parents and younger brother Shashank have an
immense contribution in publishing this book which includes their emotional and motivational support.
I look forward to kind suggestions from the valuable readers and students for further improvement in content and layout.
With best Wishes.
—Dr. Aditya Arya
 Contents
Section 1: Essential Chemistry in Biology

Chapter 1: Atomic Structure and Chemical Bonding 3–16

Chapter 2: Mole Concept and Concentration Terms 17–31

Chapter 3: Concept of pH and Biological Buffers 32–46

Chapter 4: Bioenergetics and Energy Coupling 47–65

Chapter 5: Chemical Kinetics & Colligative Properties 64–86

Model Test Paper 1:80–83

Model Test Paper 2:84–86

Section 2: Biomolecules: Structure and Function

Chapter 6: Amino Acids: Structure and Properties 89–105

Chapter 7: Proteins and their conformations 106–126

Chapter 8: Proteins: Classification and Model Examples  127–138

Chapter 9: Carbohydrates: Structure and Function 139–152

Chapter 10: Lipids: Structure, Classification and Functions 153–167

Chapter 11: Nucleic Acids: Structural Biochemistry 168–180

Chapter 12: Stabilizing Interactions in Biomolecules 181–195

Model Test Paper 1:196–198

Model Test Paper 2:199–201

Concise Biochemistry: MCQs

Section 3: Metabolism and its Regulation

Chapter 13: Global View of Metabolism 205–219

Chapter 14: Metabolism of Biomolecules 220–248

Chapter 15: Enzymes I: Principles of catalysis 249–261

Chapter 16: Enzymes II: Kinetics 262–284

Chapter 17: Enzymes III: Regulation 285–299

Model Test Paper 1:  300–302

Model Test Paper 2:303–306

 Section

1
Chapter 1: Atomic Structure and Chemical Bonding 3–16

Chapter 2: Mole Concept and Concentration Terms 17–31

Chapter 3: Concept of pH and Biological Buffers 32–46

Chapter 4: Bioenergetics and Energy Coupling 47–65

Chapter 5: Chemical Kinetics & Colligative Properties 64–86

Model Test Paper 1:80–83

Model Test Paper 2:84–86

 chap t er
Atomic Structure and
Chemical Bonding
1
Review of Some Basic Concepts
Atoms are indivisible components of a matter and therefore named so, but later it was found that atoms are consist of sub-
atomic particles called electron, neutron and proton. The discoveries of these sub-atomic particles were done using vacuum tube
experiments by JJ Thomson (Nobel, 1906), Chadwick (Nobel, 1935) and Goldstein. These discoveries helped in the elucidation
of the exact structure of an atom through a series of experiments. Chronologically, JJ Thomson proposed Plum pudding model,
Rutherford (through gold foil experiment) proved central position of nucleus, Neils Bohr (after analysing atomic spectra of hydrogen)
proposed definite position of electronic orbits and most recently Quantum mechanical model was proposed for various researchers.
Understanding of atomic structure is critical in biology to decipher the basic properties of biomolecules. Infact among 118 known
elements today only 4 elements (H, O, N, C) constitute 96.5% of the weight of living beings. The next important thing that was
revealed in chemistry was chemical bonding. Primarily, chemical bonds may be strong or weak depending upon the amount of energy
needed to break them apart. However, the secret behind biological role of these chemical entities lies in the chemical bonding itself.
Unlike chemistry, where weaker interactions are often ignored, functions of biomolecules are affected drastically on changing the
pattern of weak interactions. Different interactions have different distance dependence. The interaction most affected by distance
between atoms are vanderwaals repulsion forces.

Useful information
1. Formula for calculating

2π 2me 4 Z 2 Z2
En = − = − 13.6 eV
n 2h 2 (4πε0 )2 n2

Here m is the is the mass of electron 9.109 3 10–28 g, Z is the mass number, e is the charge on electron, h is the planks
constant- 6.62 3 10–27 g cm2 s–1 and n is the orbit number.
The energies of electrons in the Bohr’s orbits of hydrogen atom expressed in eV are:
Orbit Energy
1 –13.6/12 5 –13.6 eV
2 –13.6/22 5 –3.4 eV
3 –13.6/32 5 –1.51 eV
4 –13.6/42 5 –0.85 eV

2. Radius of the first orbit

n 2h 2 1 n2
radius of orbit = r = × = 0.529 × Å
4p 2me 2 Z Z

3
 Concise Biochemistry: MCQs
c. 247 cal / mole
d. – 247 cal/mole
64. The Gibbs free energy of binding of a ligand
with a protein is determined using calorimetric
measurements at 25°C. The value of DG ° thus
determined is 1.36 kcal/mole. The binding constant
for the ligand-protein association is:
 [CSIR-NET DEC 2012]
a. 1.30 3 10 –12
b. 0.10
c. 1.00
d. 0.97
65. t½ of an irreversible first order reaction, S → P is
1 hour. The time (in hours) require to reach 75%
completion is
 [CSIR-NET June 2013]
a. 1.5 b.  2.0
c. 2.5 d. 3.0.
66. The internal energy of a gas increases by 1 J when
it is compressed by a force of 1 Newton through
2 metres. The heat change of the system is
[CSIR NET June 2014]
a. 1 J b. –1 J
c. 2 J d. –2 J
67. DG for the base pairing of oligonucleotides (n 5 5)
at 300 K is –180 KJ mol–1. What would be the
approximate value of the equilibrium constant K?
 [CSIR-NET June 2014]
a. 100
b. 10
c. 1000
d. 1
68. The reaction of glutamate and ammonia to
glutamine and water has value 114 KJ mol for
DG °. This is coupled with the ATP reaction (ATP 1
H2O 5 ADP 1 phosphate). The DG ° (k Jmol–1) for
the coupled reaction (Glutamate 1NH3 1 ATP 5
Glutamine 1 ADP 1 Phosphate) under equilibrium
condition is [CSIR-NET June 2014]
a. 16 b. –44
c. –16 d. 44
54
69. Phosphoglucomutase is added to 0.1 M glucose-6-
phosphate (G-6-p), the standard free energy change of
the reaction, G-6-P  G-1-P is 1.8 kcal/mole at 25°C.
The equilibrium concentration of G-6-P and G-1-P
respectively are
a. 95 mM, 4.5 mM
b. 100 mM, 0 mM
c. 4.5 mM, 95 mM
d. 0 mM, 100 mM
70. The value of equilibrium constant for an
electrochemical cell reaction is 10 and its standard
e.m.f. is 0.018 V at 298 K. The number of electrons
transferred in the overall cell reaction is
[IIT-JAM 2011]
a. 2 b. 1
c. 4 d. 3
71. NAD and NADP are two important cellular electron
carriers. NAD is generally associated with catabolic
reactions and NADP with anabolic reactions. A cell
will have a fixed number of NAD molecules and a
fixed number of NADP molecules. In a normal cell
most of the: [IIT-JAM 2013]
a. NAD molecules will be in reduced state
b. NAD molecules will be in the reduced state
whereas most of the NADP molecules will be in
the oxidised state.
c. NADP molecules will be in the reduced state
whereas most of the NAD molecules will be in the
oxidised state.
d. NAD and NADP will be the oxidised state
72. In a typical cell at 378C the concentration of ATP 5
8 3 1023 M, ADP 5 1 3 1023 M, and Pi 5 8 3 1023
M. What is the actual free energy change (DG’) for
ATP hydrolysis under these conditions? [DGo’ 5 31.0
kJ mol21]
a. − 49 kJ/ mol b. 1 49 kJ/ mol
c. – 31.2 kJ/ mol d. 1 31.2 kJ/ mol
73. The conversion of A to E is coupled by the two
reactions below:
2A 1 B ↔ 2C 1 2D DG8’5 1 15 kJ/mol
C 1 D ↔ E DG8’ 5 235 kJ/mol
What is the net Gibbs free energy change for the
reaction 2A 1 B ↔ 2E
 Chapter 4: Bioenergetics and Energy Coupling

a. 250 kJ/mol 80. A thermodynamic system may go from one state to

b. 255 kJ/mol another by different paths. Which of the following
quantity/quantities is/are independent of the path?
c. 220 kJ/mol
 [HCU Biochem 2014]
d. 270 kJ/mol
a. DQ
74. What form of nucleotide represents the major energy b. DH
currency of a cell? [HCU Animal Biotech 2010] c. DW
a. Adenosine-5’- Phosphate d. DU
b. 3’, 5’- cyclic adenosinemonophosphate
81. Predict the sign of DH and DS for the following
c. 2’-o- methyladenosine
reaction:  [HCU Biochem 2015]
d. Adenosine- 5’,5’- diphosphate
2Cl  Cl2 (g)
75. When DG is negative, the reaction is a. DH and DS are positive
 [HCU Animal Biotech 2010] b. DH is negative and DS is positive
a. Exothermic b. Endothermic c. DH is positive and DS is negative
c. Hypothermic d. Ectothermic d. DH and DS is negative
76. Hydrolysis of ATP molecule to ADP releases ----- 82. Reaction with positive standard free energy change
calories of energy [HCU Animal Biotech 2011] (DG > 0) are routinely carried out by living organisms.
a. 730 This is because [HCU Biochem 2015]
b. 7300 a. Providing energy in the form of ATP hydrolysis
c. 68600 b. Coupling it to other exergonic reaction
d. 73000 c. Using enzymes to decrease DG
d. Maintaining favorable local concentrations of
77. The Free energy change DG:
substrate and products
 [HCU Animal Biotech 2012]
a. Is directly proportional to the standard free energy 83. The standard cell potential (E8cell) of the reaction
change, DG8 below is 10.126 V. The value of DG8 is
b. Is equal to zero at equilibrium  [HCU Biochem 2016]
c. Can only be calculated when the reactant and X (s) 1 2H1(aq)  X 21(aq) 1 H2 (g)
products are present at 1mol/L concentration a. 224 kJ mol21
d. Is equal to - RTlnKeq b. 124 kJ mol21
c. 212 kJ mol21
78. DG8 in a biochemical reaction represents
 [HCU Animal Biotech 2016] d. 112 kJ mol21
a. Free Energy change 84. The common currency of energy in the biological
b. Equilibrium constant reaction is [BHU Biochem 2011]
c. Standard free energy change a. AMP
d. Redox potential b. ATP
c. ADP
79. When DG8 is negative, the reaction is
 [HCU Biochem 2014] d. UDP
a. Endergonic 85. In oxidative phosphorylation, the ATP production and
b. Exergonic respiratory chain are linked by [BHU Biochem 2012]
c. Catabolic a. Chemical methods
d. Anabolic b. Physical methods

55
 Concise Biochemistry: MCQs
c. Chemiosmotic methods
d. Conformational changes
86. Entropy in a biological system does not increase
because:  [BHU Biochem 2012]
a. It is an open system
b. It is closed system
c. It is governed by vitalism
d. It is related to thermodynamics
87. The entropy change for the melting of ice is
 [BHU Biochem 2014]
a. 1ve b. 2ve
c. Zero d. No change
88. After dissolution of iodine in a solution the entropy
 [BHU Biochem 2015]
a. Increases
b. Decreases
c. First Increases then decreases
d. First decreases then increases
89. The standard free energy change (DG8, in kJ mol21) of
ATP hydrolysis obtained from the following reactions
is __________. Glucose 1 ATP ↔ Glucose-6-
phosphate 1 ADP; DG8 5 216.7 kJ mol21. Glucose-
6-phosphate ↔ Glucose 1 Pi; DG8 5 213.8 kJ mol21
 [IIT JAM 2015 –BT]
a. 1 2.9 kJ mol21
b. 22.9 kJ mol21
c. 230.5 kJ mol21
d. 1 30.5 kJ mol21
90. The energy of oxidation of glucose to H2O and CO2 is
22870 kJ mol21. The number of 700 nm photons that
must be absorbed to fix one mole of CO2 to glucose
is __________. [Given, the Planck’s constant (h) 5
6.63 3 10234 Js, the speed of the light in vacuum (c) 5
2.998 3 108 ms21, Avogadro’s number (N) 5 6.02×1023].
 [IIT JAM 2015 –BT]
a. 1.67 3 10 25
b. 8.67 3 10 25
c. 1.67 3 10 27
d. 1.67 3 10 23
91. For the Na1 mediated active transport of a molecule
of glutamic acid from a concentration of 0.1 mM
outside the cell to 20 mM inside the cell, calculate the
56
minimum number of Na1 ions required to supply the
necessary free energy. Use T 5 37°C, pH 5 7, DY 5
270 mV and F 5 23062 cal/mol.V. DG released for
the transport of one Na” is 3.3 kcal/mol. Glutamic acid
carries a net charge of 2l at pH 7.
 [IIT JAM 2013 –BT]
a. 4
b. 10
c. 2
d. 1
92. NAD and NADP are two important cellular electron
carriers. NAD is generally associated with catabolic
reactions and NADP with anabolic reactions. A cell
will have a fixed number of NAD molecules and a
fixed number of NADP molecules. In a normal cell
most of the: [IIT JAM 2013 –BT]
a. NAD and NADP molecules will be in the reduced
state
b. NAD molecules will be in the reduced state
whereas most of the NADP molecules will be in
the oxidized state
c. NADP molecules will be in the reduced state
whereas most of the NAD molecules will be in the
oxidized state
d. NAD and NADP molecules will be in the oxidized state
93. A system at equilibrium under conditions of constant
temperature and pressure, which one of the following
will be minimum? [TIFR NCBS 2013]
a. Enthalpy
b. Entropy
c. Gibbs free energy
d. Volume
94. Given the following values of DH and DS, which one
of the following processes can take place at 3008 K
without violating the second law of thermodynamics?
 [TIFR NCBS 2013]
a. DH: 220 Kcal Mol21 DS: 180 Kcal Mol21 K21
b. DH: 220 Kcal Mol21 DS: 280 Kcal Mol21 K21
c. DH: 120 Kcal Mol21 DS: 130 Kcal Mol21 K21
d. DH: 120 Kcal Mol21 DS: 230 Kcal Mol21 K21
95. In which of the following reactions there is an
increase in entropy [TIFR NCBS 2015]
a. Condensation of water
b. Polymerization of agarose gel
 Chapter 4: Bioenergetics and Energy Coupling

c. Combustion of paper a. 5.7

d. Compression of Hydrogen b. 6.7
c. 10.4
96. Hydrolysis of ATP over ADP and AMP generates
highest energy because [DBT JRF 2011] d. 3.8
a. ATP on hydrolysis generates thermodynamically 99. The standard free energy change (∆G0) for ATP
stable structure hydrolysis is -30 kj.mole21. The in vivo concentrations
b. ATP is highly unstable of ATP, ADP and Pi in E. coli are 7.90, 1.04 and 7.90
c. Hydrolysis of ATP is pH dependent mM, respectively. When E. coli cells are cultured at
37 8C, the free energy change (∆G) for ATP hydrolysis
d. Hydrolysis of ADP and AMP do not generate
in vivo is ----------KJmole21. [GATE BT 2015]
thermodynamically stable structure
a. 130 kJ
97. The equilibrium constant (Keq) for the reaction S ↔ b. 230 kJ
P is 5. Suppose we have a mixture of [S] 5 2 3 1024
c. 1 301 kJ
M and [P] 5 3 3 1024 M. In which direction will the
reaction proceed on addition of appropriate enzyme? d. 2301 kJ
[DBT JRF 2011]
100. Calculate the standard free-energy changes of the
a. Proceeds in a forward direction following metabolically important
b. Proceeds in a reverse direction Enzyme-catalyzed reactions at 25°C and pH 7.0 from
c. Proceeds in both the directions the equilibrium constants given.
d. Proceeds sometimes in forward and sometimes in Glutamate 1 oxaloacetate ↔ aspartate 1
reverse direction a-ketoglutarate K’eq 5 6.8.
a. 14.76 kJ/mol
98. Triose phosphate isomerase converts dihydroxy
acetone phosphate (DHAP) to glyceraldehyde3- b. 24.76 kJ/mol
phosphate (G-3-P) in a reversible reaction. At 298 K c. 213.86 kJ/mol
and pH 7.0, the equilibrium mixture contains 40 mM d. 113.86 kJ/mol
DHAP and 4 mM G-3-P. Assume that the reaction
started with 44 mM DHAP and no G-3-P. The standard
free-energy change in kJ/mol for the formation of
G-3-P [R 5 8.315 J/mol.K] is _________
 [GATE BT 2014]

The concept of free energy may help us to know the possibility of occurrence of Biochemical reactions, as well as transport across
membranes and concentration dependence of the reactions. We may also use all thermodynamic relations to predict the number
of electrons involved, or desired concentration needed to carry out a reaction spontaneously. Here in this question let us try to find
out requirement of protons in a secretory process using bioenergetics principles The H1 concentration in gastric juice is 0.1M.
The protons arise from blood, which has a pH of 7.4. Calculate the free energy change required for transport of enough protons to
produce 1 litre of gastric juice at 37°C.

57

63. Which of the following mutations will be most
damaging to the structure of a protein
a. A 198 V b. C 185 T
c. R 187 K d. E 176 H
64. Popai, a scientific advisor of nina, went to moon
and obtained few proteins on the lunar surface.
When he returned to earth somehow, change in
the environment, few amino acids got modified by
chemical conversions which of the following changes
in amino acids would have led to maximum alteration
in the structure
a. Serine to Threonine
b. Leucine to Isoleucine
c. Glutamate to Isoleucine
d. Histidine to Arginine
65. Which of the following amino acids are most likely
to undergo glycosylation during post translational
modifications
a. Serine, Threonine, Asparagine
b. Serine, Threonine, Arginine
c. Serine, Arginine and Glutamine
d. Cysteine, Serine and Histidine
66. Ninhydrin test is given by [HCU Animal Biotech 2010]
a. Carbohydrates
b. Proteins
c. Alkanes
d. Alkenes
67. At physiological pH, the carboxyl and amino groups in
an amino acid are in the following form
 [HCU Animal Biotech 2010]
a. COO2, NH2
b. COOH, NH2
c. COOH, NH31
d. COO2, NH31
68. Which of the following is an essential amino acid
 [HCU Animal Biotech 2010]
a. Alanine
b. Threonine
c. Aspartic acid
d. Glycine
Chapter 6: Amino Acids: Structure and Properties
69. The amino acid sequence of a peptide Q-W-E-D is
 [HCU Animal Biotech 2010]
a. Tryptophan-Glutamine-Glutamate-Aspartate
b. Glutamine-Tryptophan-Aspartate-Glutamate
c. Glutamine-Tryptophan-Glutamate-Aspartate
d. Glutamate-Tryptophan-Glutamine-Aspartate
70. Which of the following amino acids does not undergo
phosphorylation [HCU Animal Biotech 2010]
a. Serine b. Threonine
c. Tyrosine d. Alanine
71. The amino acid leucine has the following side chains
 [HCU Animal Biotech 2011]
a. CH3-CH2(CH)2-
b. (CH3)2-CH-CH2-
c. CH3-CH (OH)-
d. CH3-CH2-CH(CH)-
72. Which of the following is an acidic amino acid
 [HCU Animal Biotech 2011]
a. Asparatic acid
b. Isoleucine
c. Lysine
d. Proline
73. Histones have high content of amino acids such as
 [HCU Animal Biotech 2016]
a. Arginine and lysine
b. Tryptophan and leucine
c. Glutamine and Asparagine
d. Phenylalanine and histidine
74. Which of the following amino acids is not optically
active? [HCU Biochemistry 2015]
a. Lysine b. Alanine
c. Glycine d. Tyrosine
75. Which of the following pairs of amino acids could
form a salt bond at pH 7.4?
 [HCU Animal Biotech 2015]
a. Glycine and Arginine
b. Valine and Lysine
c. Leucine and Histidine
d. Glutamate and Arginine
95
 Concise Biochemistry: MCQs

76. Amino acids that does not contain hydroxyl group in 82. The majority of amino acid in histones in eukaryotes
their side chains is [HCU Biochem 2016] are [BHU Biochem 2010]
a. Serine a. Aromatic in nature
b. Threonine b. Basic in nature
c. Tyrosine c. Acidic in nature
d. Histidine d. Hydrophobic in nature

77. pK1 (2COOH), pK 2 (2NH31) and pK3 (side chain) of
Asparatic acid are 1.88, 9.6 and 3.65 respectively. At
which pH asp will not move in electric field?
 [HCU Biochem 2016]
a. 5.75
b. 2.77
c. 6.6
d. 6.0
78. In a sample consisting of lysine, leucine and glutamic
acid, which will be eluted first from a cation exchange
resin at pH 1. [HCU Biochem 2016]
a. All the three will be eluted at the same time
b. Lysine
c. Leucine
d. Glutamic acid
79. What would be the structure of histidine at pH 8.
 [HCU Biochem 2016]
a. b. 86. The protein are constituted by
c. d. b. D amino acids only
83. Glycine is unique in the sense
 [BHU Biochem 2011]
a. It is unreactive amino acid
b. It is optically active
c. It is optically inactive
d. It has aromatic side chain
84. The amino acid found in the active site of enzyme is
commonly [BHU Biochem 2011]
a. Methionine b. Lysine
c. Arginine d. Histidine
85. Isoelectric point is a point at which
 [BHU Biochem 2011]
a. The mass of a protein is maximum
b. The net charge of protein is zero
c. The speed of mobility is maximum
d. The protein loses structure
 [BHU Biochem 2011]
a. Both L and D amino acids
c. L amino acids Only
d. Depends on the type of protein

80. One of the following is not a cryoprotectant? 87. The Guanidino group is found in
 [BHU Biochem 2010]  [BHU Biochem 2011]
a. Dimethylsulphoxide a. Tryptophan
b. Proline b. Leucine
c. Sucrose c. RNA/DNA
d. Glycine d. Arginine

81. One letter code for the glutamine is 88. Amino acid that most often occurs at the active
 [BHU Biochem 2010] site of enzymes and can be uncharged or positively
a. P charged depending on its local environment
 [BHU Biochem 2011]
b. A
a. R b. H
c. Q
c. K d. D
d. G

96

37. Here we should remember that if G1C content
in double stranded DNA is 68%, this means
remaining 32% will be AT and when this DNA
will transcribe into RNA only one of the strand
will be transcribed which means all the G will
form C in mRNA and all the C will form G in
m-RNA and also GC of one strand would be equal
to GC of other. So if we understand this using
some sample values (such as 68 bp out of 100
are GC in both stands, so in one of the strand 34
out of 50, which means 34%of whole DNA ) but
if only one strand will be transcribed, RNA will
have 34 GC among 50. So percentage will be
68% correct answer is a.
38. Option c will be correct as stated in Szybalski’s
rule, A 1 T may not always be equal to G 1 C.
39. Mole fraction can be calculated on the basis
of basic definition, mole fraction of second
component will be 1 minus mole fraction of other.
So answer to this question will be 1 – 0.36 5
0.64
40. As in the second strand A5G and T5C and
therefore in second strand (T1C)/ (A1G) will be
0.7 (as A in first strand 5 T in other strand on so
on.). So the reverse ratio will be (A1G)/T1C) 5
1/0.7 5 1.43
52. It should be noted that addition of Ethidium
bromide causes the shift in structure of DNA
to Z-form due to intercalation. Also, the binding
of EtBr is known to reduce the density of DNA,
which forms the basis of DNA separation using
density gradient centrifugation.
59. First we may determine the number of residues
in protein i.e. 40,000/110 5 363.6 amino acids
or 364 aa. Now, each amino acid is encoded
by a triplet of nucleotides, so total number of
nucleotides 5 364 3 3 5 1092 base pairs.
Average molecular weight of nucleotide 5 650
dalton
Hence, the molecular weight of a DNA will be
650 3 1092 5 709800 .
Chapter 11: Nucleic Acids: Structural Biochemistry
60. Similar to previous question the total DNA in
Answer Key and Solutions
a cell is 3.2 x2 5 6.4 3 109 base pairs (diploid
cell). Now as this DNA is divided into a set of
23 pairs (or 46 ) chromosomes, so total DNA per
chromosome 5 6.4 3 109 / 46 5 1.391 3 108 bp
Mol wt of each chromosome 5 1.391 3 108 3 650
5 9.043 3 1010 Dalton or 9 3 107 kDa = 90 million
kDa.
84. Calculate using chargaff’s rule A 5 15.1. so AT 5
30.2 remaining is GC i.e 100-30.2 5 69.8
And as G5C so G 5 69.8/2 5 34.9
85. Average molecular weight of a nucleotide is
considered as 650 dalton, so the number of
nucleotides in DNA with 3 3 107 dalton would be
3 3 107 / 650 5 4.61 3 10 4 bp
The helical rise per base pair in DNA is
3.4 angstrom or 3.4 3 1024 μm . Hence
the length of 4.61 3 104 bp DNA will be
4.61 3 10 4 3 3.4 3 1024 5 15.67 . There was no
precise option, yet the closest answer is 16.5.
86. The exact average used in most of the
biochemistry text is 660 dalton or 650 Dalton for
a nuclotide pair and for a nulceotide it is 325 or
330, but for a base which exludes the phosphate
and sugar is around 240 dalton
88. Dicer, also known as endoribonuclease Dicer
or helicase with RNase motif, is an enzyme
that in humans is encoded by the DICER1 gene.
Being part of the RNase III family, Dicer cleaves
double-stranded RNA (dsRNA) and pre-microRNA
(pre-miRNA) into short double-stranded RNA
fragments called small interfering RNA and
microRNA, respectively.
100. Total bases of DNA 5 2000 (1000 bases in each
strand)
Total no. of Adenine 5 750 (75% of 1000) 1 100
(10% of 1000) 5 850
in each strands, A will pair with T in another
stand. So, 850 AT pairs in total therefore only
150 (1000-850) G1C pairs will be present in both
strands of DNA. So All 850 adenine- thymine
pairs will form 850 3 2 5 1700 H bonds, and
All GC will form 150 3 3 5 450 hydrogen
bonds. So total number of bonds will be
1700 1 450 5 2150.
179
 Concise Biochemistry: MCQs

Puzzle : Try solving this puzzle to revise basic concepts

Answer Key and Solutions

Across Down

4. This nitrogenous base has highest number of 1. The type of sugar which is preset in nucleic acids
atoms
2. The handedness of the Z DNA helix is .......
6. A clinician who made the discovery of nuclein handed
from used bandages containing pus.
3. A nitrogenous base with one ring in its structure
7. A nitrogenous base with two rings in its structure
5. This base in present in RNA but not in DNA
9. The phenomenon of change in plane of atoms of
ribose in nucleic acids is called ? 8. The number of torsion angles in polynucleotide is
... (write in words)
10. A scientist who suggested that nucleic acid is
repeating tetramer

9 10

180
 chapt er
Stabilizing Interactions in
Biomolecules
12
Review of Some Basic Concepts
Biomolecules are stabilized by a number of strong and weak interactions. As we leant in the first chapter that weak interaction play
a dominant role in stability of biomolecules and they are primarily responsible for their biological activity, or they are responsible
making a molecule – biomolecule, else the elemental composition is similar in many non-living entities. In biomolecules a set of
more than covalent bonds have been given specific names such as in protein the linkage CONH is known as peptide linkage, in
carbohydrates the linkage between two sugars is known as glycosidic linkage, in lipids (fats) the linkage between glycerol and fatty
acids is known as triester linkage and in nucleic acids the linkage between successive nucleotides is known as phosphodiester
linkage. These are basic connections that are responsible for very existence of the molecules. However, interactions such as salt
bridges, hydrophobic interactions, vanderwaals interactions are other interactions which allow the biomolecules to adopt particular
shapes relevant to their biological activity. These weak interactions are largely affected by the environment surrounding them.
A change in salt concentration, change in temperature or addition of detergents can severely affect the conformation and hence
biological activity. These changes are often observed as complete loss of native structure called denaturation and then regain of
structure and biological activity called renaturation. Anfinsen, proved this phenomenon in protein using elegant experiments and
showed that information for protein folding lies in its sequence. Biomolecules may be denatured by heat or by chemical denaturants.
A large variety of chemical denaturants exist, such as acids, bases, solvents, cross linking agents, chaotropic agents and reducing
agents. Chaotropic agents (oder breaking) agents can disrupt the hydrogen bonding network between water molecules and thus
weaken the hydrophobic effect and cause denaturation e.g. urea and guanidium chloride. Kosmotropic agents (order making) on the
other hand, can increase the hydrogen bonding between the water molecules thus promoting the precipitation of biomolecules e.g.
ammonium sulphate. The chaotropic or kosmotropic nature may be compared by Hofmeister series which classify various chemical
agents on the basis of chaotropic potential. Stability of nucleic acid especially DNA is due to hydrogen bonding and heat is major
denaturant that convert the dsDNA into ssDNA. As there are 3 hydrogen bonds between G and C in contrast to 2 hydrogen bonds
between A and T, the fraction of AT or GC is primary factor that decides melting temperature of DNA. The rate of renaturation of ds
DNA follows a second order kinetics and therefore a mathematical relation shows that rate is directly proportional to the product
of initial ssDNA and time take to renature 50% of it call Cot value. Cot curves are extensively used for the analysis of genomes and
comparing the DNA complexity.

Useful Information
1. Wallace rule: Tm = 2°C (A+T) + 4°C (G+C)

2. Modified Wallace formula: Tm = 81.5 +16.6 log M +41 (χG+χC) – 500/L – 0.62 F
(Here χ is the mole fraction, L is the length of shortest strand in duplex, F is concentration of formamide)

3. C0 t1/2 = 1/k (k is the rate constant, C0 is initial conc. of denatured DNA, t1/2 time for 50% renaturation)

4. categories of various denaturants and their mechanim of precipitating biomolecules

Acetic acid, sodium bicarbonate - Ionic precipitation
Ethanol, butanol - dehydration and removal of solvation sphere
Formaldehyde, Gluteraldehyde - cross linking
Urea, Guanidium salts - chaotrophism
Mercaptoethanol, DTT - reducing agents

181
 Concise Biochemistry: MCQs
Model Test paper 1
Model Test Paper 1
  60 minutes 
Instructions: Please read before answering
1. Answers have to be marked on the sample OMR answer sheet provided as supplement with this book
2. All questions carry two mark each.
3. 0.25 mark will be deducted for every wrong answer.
4. Space for the rough work is provided at the back of sample OMR sheet
5. Non-programmable scientific calculators are permitted.
6. Cell phones are not allowed
1. Selenocystein and Pyrolysine are encoded by
which of the following codons
a. UAG and UGA respectively
b. UGA and UAG respectively
c. GUG and CUG respectively
d. AUG and CUC respectively
2. Which of the following statements is INCORRECT
for a peptide made up of 9 amino acids
a. It has molecular weight of 1008
b. It has 9 peptide bonds
c. It has 9 alpha carbon atoms
d. It has 8 phi and 8 psi angles
3. Levinthal estimated the possible number
of conformation of a peptide using simple
probability and reached to contradiction that a
protein cannot scan through all the possibilities
during the folding process. A student who was
reading his calculation had a misprint in the
book. Can you help student to know how many
possibilities peptide of 101 amino acids can have
if each peptide bond has two torsion angles and
each angle has two stable orientations.
a. 2101
b. 4101
c. 4100
d. 1004
4. The correct order of amino acids on the basis of
following properties:
Smallest, Largest, Most hydrophobic, Most
hydrophillic, Most abundant,
196
Maximum Marks 50
a. Gly, Trp, Ile, Gln
b. Gly, Ile, Gln, Trp
c. Gln, Ile, Gly, Trp
d. Gly, Gln, Trp, Ile
5. Clinically appropriate range of hemoglobin is
a. 11.5 to 13.5 g/dl for male and 13.5 to 17.5 g/dl
for female
b. 13.5 to 17.5 g/dl for male and 12.0 to 15.5 g/dl
for female
c. 8.5 to 10.5 g/dl for male and 12.0 to 13.5 g/dl
for female
d. 12.0 to 15.5 g/dl for male and 13.5 to 17.5 g/dl
for female
6. How many amino acids of the per peptide chain
of myoglobin (and hemoglobin) are involved in
interaction with oxygen and Iron respectively
a. One histidine and one arginine
b. Two histidine
c. Two Arginine
d. One Histidine and one glutamate
7. Which of the following is true about carbohydrates
a. Carbohydrates are most abundant biomolecule
on earth
b. All hydrates of carbon are carbohydrates
c. Carbohydrates are polyhydroxy aldehydes or
ketones
d. All carbohydrates are sweet in taste
8. Which of the following carbohydrate contains
beta anomeric form of glucose
 Concise Biochemistry: MCQs
22. An uncompetitive inhibitor of enzyme binds to
Model Test Paper 2
a. The active site of enzyme
b. Site other than the active site
c. Enzyme-substrate complex
d. Any other site and modifies part of an enzyme
23. Michaelis and Menten derived their equation
using which of the following assumption?
a. Rate limiting step in the reaction is the
breakdown of ES complex to product and free
enzyme
b. Rate limiting step in the reaction is the
formation of ES complex
c. Concentration of the substrate can be ignored
d. Non-enzymatic degradation of the substrate
is the major step
24. A plot of V/[S] versus V is generated for an
enzyme catalyzed reaction, and a straight line is
obtained. Indicate the information that can be
obtained from the plot.
306
a. Vmax and turnover number Km can be obtained
only from a plot of l /V versus l/[S].
b. Km/ Vmax from the slope.
c. Vmax, Km and turnover number.
d. Only Km and turnover number
25. An enzyme-catalyzed reaction was carried out
with the substrate concentration initially 1,000
times greater than the Km for that substrate.
After 9 minutes, 1% of the substrate had been
converted to product, and the amount of product
formed in the reaction mixture was 12 μmol.
If, in a separate experiment, one-third as much
enzyme and twice as much substrate had been
combined, how long would it take for the same
amount (12 μmol) of product to be formed?
a. 3 min
b. 6 min
c. 13.5 min
d. 27 min
About The Authors

Dr. Aditya Arya

Dr. Arya is a Ph.D. in the area of Nanomedicine from Defence Research and Development
Organization, Delhi. He has published 20+ research papers in peer-reviewed international journals,
four chapters in international books and authored five books. He holds membership of several
international societies in Nanomedicine, Redox Biology and has received several prestigious
awards in the domain of life science research. He has been trained at some of the prestigious
institutes such as Sanger Institute (Cambridge), EMBL (Heidelberg), Myograd (Berlin), IBRO (Paris).
He has also delivered several scientific talks at national and international platforms. He has more
than five years of teaching experience in Biochemistry with a special focus on Proteomics,
Enzymology, Metabolism, Radical Biology and Lab techniques.

Dr.Narendra Kumar Sharma

Dr. Narendra Kumar Sharma has Doctorate Degree in High Altitude Physiology and Proteomics from
Defence Research and Development Organization. At present he is working as a post doctoral
fellow at Guangzhou Institute of Biomedicine and Health, Guangzhou, China. He has done
extensive research in the domain of proteomics and has published 15+ papers, 4 book chapters
and 2 books. He is also the member of several scientific societies and editorial board member of
5+ International Journals.

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