Aim4 aiims biochemistry-free-sample

ALTISVORTEXAim4AIIMSBiochemistry
chemistry
ALTIS VORTEX
4AIIMSAim
Dr. Karthikeyan Pethusamy
Bio
800+ One-liners for quick review
445 Chapter-wise review questions
with adequate explanations.
Comprehensive, up-to-date and
easy-to-understand information
References and updates from
th
Harper 30th ed, Harrison 19 ed
Section on Image based questions
Ashikh Seethy
Senior Resident and
PhD Scholar
AIIMS-Delhi
Amar Preet Kaur
Senior Resident and
PhD Scholar
AIIMS-Delhi
Reviewers
Dr. Karthikeyan Pethusamy had completed his MBBS
with three distinctions and a gold
medal in medicine from Kanyakumari Government
Medical College. He did his
M.D. Biochemistry from Maulana Azad
Medical College, New Delhi. Currently,
he is a senior resident and PhD scholar at AIIMS, New Delhi.
About the author
Author's facebook page: Biochemistry with Karthi

Altis Vortex
New Delhi
BIOCHEMISTRY

Published By :
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Rights
All rights will be reserved by Publisher. No part of this book may be used or
reproduced in any manner whatsoever without the Written permission from
publisher.
Disclaimer : Every effort has been taken in compiling/editing of the concerned
data/information given in this book in various section, Also the questions in
this book are memory based so it is possible to remain some mistake due to
human error if so kindly compare the data with the government publication,
journals and notification.
Dr. Karthikeyan Pethusamy is a temporary employee of Department of
Biochemistry,AIIMS,NewDelhi.Anyviewsexpressedhereindonotnecessarily
represent the views of AIIMS, New Delhi.
EDITION: First (2017)
BOOK CODE : 0845
ISBN: 978-81-931706-9-4

PREFACE
Dear Reader,
This book is entirely a result of my passion for learning and teaching. So, this book is
definitely going to make your exam preparation an easy and enjoyable experience.
Standard textbooks are written with the purpose of giving a complete and detailed
knowledge of a subject but it’s quite impossible for anyone to revise that thoroughly
on a day before the exam. I felt this during my own exams, while helping students
preparing for their exams and during so many other moments. The present book is
primarily aimed to fulfill this need.
I went through various entrance exam questions and then assembled these questions
into one-liners and topic-wise review questions for an ease of revision. The answers
are written in the way I teach my students i.e. addressing their relevant doubts. These
were sourced from the standard textbooks. I strongly believe that this book is going to
be very helpful for a quick revision for the different entrance exams i.e. PGMEE, first
professional MBBS exams and other exams like CSIR-UGC-NET as well.
The content of the book has undergone a very rigorous quality control process as even
a single mistake in the book can drastically affect the student’s rank in entrance exam.
If you feel that any information is incorrect or incomplete, you are most welcome to
contact me through my Facebook page – Biochemistry with Karthi. Errors in the book,
if any will always be accessible to you through my Facebook page.
In this book, there are a few tricky questions which may not even come in exams. The
sole purpose of those questions is to kindle your interest and develop an interest in the
subject.
I commit to update the information in the book once in a year to include the latest
questions. If you are reading an old edition, you can always request me for updates of
the new edition. I will be happy to provide you.
Happy studying! Stay blessed!
Dr. Karthikeyan Pethusamy M.D. 03-03-2017
Senior Resident & PhD Scholar
Department of Biochemistry
AIIMS, New Delhi.

ACKNOWLEDGEMENT
Reviewers:
• Dr. Ashikh Seethy M.D., Senior resident & PhD scholar, AIIMS, Delhi.
• Dr. Amarpreet Kaur M.D., Senior resident & PhD scholar, AIIMS, Delhi.
Help in proof-reading:
• Mr. Akshay Munjal M.Sc, Biochemistry, AIIMS, Delhi
• Dr. Ankita Raj, M.D Biochemistry, AIIMS, Delhi
• Mr. Dhruv Das, M.Sc, Biochemistry, AIIMS, Delhi
• Dr. Diravyaseelan M, M.D Biochemistry, AIIMS, Delhi
• Miss. Indrani Mukherjee, Junior Research Fellow, AIIMS, Delhi
• Dr. Prajwal Aathreya M.D Biochemistry, AIIMS, Delhi
• Mr. Rahul Yadav, M.Sc, Biotechnology, AIIMS, Delhi
• Mr. Sunil Singh S, M.Sc, Biochemistry, AIIMS, Delhi
• Dr. Vijayalekshmi B, M.D Biochemistry, AIIMS, Delhi
• Dr. Pankhuri Dudani MBBS, MAMC, Delhi
• Dr. K. Kritika M.D., Senior resident, MAMC, Delhi
• Dr. Manjeet Goyal, VMMC, Delhi
My UG teachers of Biochemistry:
• Dr. Vijayalakshmi M.D.
• Dr. Lalita M.D.
My PG teachers of Biochemistry:
• Prof. Dr. Sarita Agarwal
• Prof. Dr. Alpana Saxena
• Late. Prof Dr. P.C. Ray
• Prof. Dr. S.K.Gupta
• Prof. Dr.T.K. Mishra
• Prof. Dr. P.Lali
• Prof. Dr. B.C. Koner
• Prof. Dr. Lal Chandra

• Prof. Dr.Smita Kaushik
My PhD mentor:
• Dr. Subhradip Karmakar, PhD, Assistant professor, AIIMS, Delhi
My seniors and friends who are my source of inspiration:
• Dr. Montosh Chakroborty – Assistant professor, Andaman & Nicobar Islands
Institute of Medical Sciences
• Dr. Radhey Natung M.D, Biochemistry
• Dr. Pinky Garg – Associate professor, North DMC Medical College & Hindu Rao
Hospital
• Dr. Maheshwari K – Assistant Professor, JIPMER, Karaikal,
• Dr. Dnyanesh Amle, Pt. J.N.M. Medical College, Raipur
• Dr.Sagar Dholaria, Assistant professor, R.D.Gardi medical college, Ujjain
• Dr. Selvakumar Kingslin, M.D., Anaesthetist, Thiraviyam Hospital, Nagercoil
• Dr. Thambi David, M.Ch., Pediatric surgeon, Kanyakumari government Medical
College
• Dr. Vineet Sehgal, Glaucoma Specialist, Sharp Eye Centre, Delhi
• Dr. Jhuma Das, Senior resident, MAMC, Delhi
• Dr. Ayush Jain, M.D (radio), Seth GS Medical College, Mumbai
Students who inspired me to come up with this book:
• Dr. Ashwin AJ, Third MBBS, Government Villupuram Medical College
• Dr. Naveen Kumar, Third MBBS, Stanley Medical College
• Dr. Rushikesh Ghongade, Final MBBS, IGGMC, Nagpur.
• Dr. Preeti Joon, Final MBBS, Grant Medical college, Mumbai.
• Dr. Abhishek V J, Malankara Orthodox Syrian Church Medical College, Ernakulam.
• Dr. Nirav Mungalpara, Baroda Medical College, Gujarat
All my batchmates and juniors from Kanyakumari government medical college
All my students in MAMC for their love and support. It was my fortune to teach
them.
To my parents and family
Altis Vortex team:
• Dr. Ajay Mohan
• Mr. Vinod Kumar
• Mr. Anit Rana

ABOUT THE AUTHOR
Dr. Karthikeyan Pethusamy had completed his MBBS with three
distinctions and a gold medal in medicine from Kanyakumari
Government Medical College, Nagercoil, Tamilnadu.
He took Biochemistry by choice. He was the first one to take
M.D. Biochemistry in All India Counseling 2012. He has joined
AIIMS as an SR and PhD scholar after completing his MD from
MAMC, New Delhi. He did his thesis under the mentorship of Dr.
Sarita Agarwal on the effect of gene polymorphisms in stroke.
Currently, he is studying the epigenetic changes in AML.
He is popular among his students for his clarity and student
friendly method of teaching. His grip on all subjects is firm, and
he brings it into the teaching of the subject of his choice-
Biochemistry. He is also engaged in teaching students in virtual
platforms like Whatsapp and Facebook. He has authored and
coauthored many exam-oriented Biochemistry books.
Besides Biochemistry, he loves nature. He has been riding bicycle
to commute around for the past 10 years and motivates others to
do the same. During his tenure as Green Care Secretary of
Kanyakumari Government Medical College, he was instrumental
in planting around 1000 trees in his vast college campus.
He is an active contributor to Tamil Wikipedia and Quora.
Writing scientific books in Tamil and starting an NGO that will
work for environmental conservation projects are his two dream
projects.

How to make the most of this book?
One-liners section is for the rapid-review before the exam. This will
be your elev-enth-hour-Samaritan. Don’t forget to go through this a day
before exam once you have gained adequate knowledge of
Biochemistry.
Assess yourself tables have been introduced to avoid the boredom that
may arise when you read one-liners continuously. Hide the right-side of
the table and try to answer.
Most-common, Most-abundant, Pioneer scientists in Biochemistry
and Biochemical tests are condensed information that I have made after
spending so many hours. Use these sections to save your time.
Solved AIIMS questions will show you how to approach a question in
any exam and how to rule-out the incorrect options logically. In some
questions, I have shown you how to derive the answer even if you don’t
know the answer.
YouTube video links are given for certain questions. This will take you
to my YouTube channel – Biochemistry with Karthi where I’ve upload
the exam-oriented videos. A word of caution: Don’t get distracted by
other videos on YouTube. You have an exam to excel.
Chapterwise review questions with explanations are quite important
to build your concepts. Once you have completed a chapter from a
textbook or after a class, try to solve the questions. If you don’t know
the answer, refer to the explanations and the textbook reference I’ve
mentioned. Questions are of high-standard and exam-oriented.
Biochemistry with Karthi Facebook page is a way to contact to me
and get to know the updates about the subject. I regularly post new and
interesting questions in the page.
To be honest, this book is primarily meant as a supplement. This
is not an all-in-one solution for Biochemistry. So, I strongly suggest
you to read any of the following textbooks.
Text books I personally suggest: (any one)
• Harper’s Illustrated Biochemistry – 30th edition
• Lippincott’s Illustrated Reviews: Biochemistry, 6th edition
• Textbook of Biochemistry 8th Edition by D M Vasudevan S

This is a sample e-copy of the book.
To get a printed book, kindly visit:
https://www.aim4aiims.in/pg/buy-product.php?id=73
Errata of the book can be accessed here:
https://www.facebook.com/notes/biochemistry-with-
karthi/errata-of-aim4aiims-biochemistry/294306637648890

CONTENTS
Last-Minute Revision
1. One-liners 1
2. The Most Common 48
3. The Most Abundant 52
4. Pioneers in Biochemistry 53
5. The First in History 55
6. Biochemical Tests 56
AIIMS Solved Questions
7. AIIMS May 2016 57
8. AIIMS Nov. 2015 69
Self-Assessment & Review questions with adequate explanations
9. Chemistry of Carbohydrates 90
10. Enzymology 98
11. Metabolism of Carbohydrates 109
12. Chemistry of Amino Acids & Proteins 129
13. Metabolism of Amino Acids 135
14. Heme Metabolism 151
15. Lipid Chemistry & Metabolism 159
16. Nucleotide Chemistry & Metabolism 175
17. Free Radicals and Antioxidants 186
18. Xenobiotics Metabolism 189
19. Molecular Biology 194
20. Immunology 229
21. Cytoskeleton and Muscle Biochemistry 243
22. Nutrition 248
23. Image Based Questions 252
24. Questions & Answers
24.1 Hemoglobin & Myoglobin 258
24.2 Cell membrane and Transport 260

Author's facebok page: Biochemistry with Karthi

One-Liners
Last Minute Revision
Physical Chemistry, Water & Electrolyte, Acid-base balance
• pH = - log10
[H+
] in moles/litre
• pH= pKa+ log10
Salt
Acid
[ ]
[ ]
(Henderson–Hasselbalch equation)
• Solvent property of water is because of its ability to make hydrogen bonds
with solutes.
• A buffer is most effective when the pH is equal to the pKa of the buffer, i.e.
[salt] = [acid] (full ionisation)
• Effective pH range of a buffer = pKa ± 1
• Bicarbonate buffer system (H2
CO3
/HCO3
-
) is 'open at both ends' since the
level of both the constituents of this buffer can be altered by the body.
• Glutamine is the source of NH3
in the kidney.
• Unequal distribution of diffusible ions between two compartments separated
by a semi-permeable membrane when a non-diffusible ion is present in one
of the compartments is due to Gibbs-Donnan-membrane equilibrium.
• Higher chloride concentration in Cerebrospinal fluid compared to plasma
can be explained by Gibbs-Donnan membrane equilibrium.
Normal pH range of blood 7.35–7.45
Normal pH range of urine 6.5-7
pKa of albumin 5.8
Critical acidifying capacity of kidney
i.e. limiting urinary pH
4.5
Major extracellular buffer Bicarbonate buffer
Major intracellular buffer Phosphate buffer
Major urinary buffer Phosphate buffer
Isocapneic buffering in endurance
training is due to
Increased CO2
but normal pCO2

The Most Common
Gene disorder worldwide Thalassemia
Enzyme deficiency (enzymopathy) G6PD (mostly asymptomatic)
Qualitative Hemoglobinopathy Sickle cell anemia
Mutation in cystic fibrosis
Δ F508 (Deletion of phenylalanine at
508th
position)
Viable chromosomal disorder Down syndrome (21 trisomy)
2nd
most common autosomal trisomy
resulting in live birth
Edward syndrome (18 trisomy)
Mutation in galactosemia in Cauca-
sian
Q188R (replacement of glutamine by
arginine)
Gene mutated in congenital adrenal
hyperplasia
CYP21A2 (21-α hydroxylase)
Gene mutated in congenital hearing
loss
Connexin 26
Mutation leading to permanent neo-
natal diabetes
KCNJ11 (ATP sensitive K+
channel)
Inherited urea-cycle defect OTC deficiency
SCID X-linked SCID
Saturated fatty acids present in the
cell
Palmitic acid (C16) and stearic acid
(C18)
Type of plasma membrane receptor GPCR (G-Protein Coupled receptor)
Type of prosthetic groups, cofactors
for enzymes
Metal ions
Covalent modification regulating en-
zyme activity
Phosphorylation-dephosphorylation
Fatty acid in natural fats Oleic acid

The Most Abundant
Amino acid in plasma Glutamine
Anterior pituitary hormone Growth hormone
Biological forms in the world Polysaccharides
Nucleoprotein Histone
Type of collagen in basement membrane Type IV
Type of collagen in the body Type I
Type of collagen in the cartilage (except
white fibro cartilage)
Type II
Type of collagen in the bone and white
fibrocartilage
Type I
Constituent of body Water
Free nucleotide in mammalian cells ATP
Glycoprotein in basement membrane Laminin
Glycosaminoglycan Chondroitin sulphate
Heteropolysaccharides in the body Glycosaminoglycan
Immunoglobulin IgG
Ketone body during ketosis β-hydroxy butyrate
Lipid in chylomicron Triacylglycerol
Membrane proteins of RBC
Glycophorin & Band 3 anionic
transporter
Osmotically active component of the plasma Sodium
Peripheral membrane protein of RBC Spectrin
Platelet receptors GPIIb-GPIIIa complex
Prokaryotic DNA polymerase DNA polymerase I
Protein in HDL
Apo A-I (70% of weight)
followed by Apo AII
Protein in the human body Collagens
Saturated fatty acid in circulation Palmitic acid
Sigma factor in E. coli Sigma 70
Stop signal for transcription termination RNA hairpin
Tocopherol in extrahepatic tissues α-tocopherol

Pioneers in Biochemistry
Alec Jeffreys DNA fingerprinting
Andrew Fire & Craig
Mello
siRNA
Arber, Smith & Na-
thans
Restriction enzymes
Arthur Kornberg DNA polymerase
Avery, Macleod &
McCarty
DNA is the information molecule/genetic
material
Barbara Mcclintock Transposons
Blobel Signal sequence hypothesis
Dorothy Hodgkin Protein crystallography
Frederick Sanger Sequencing of 1° structure of bovine insulin &
sequencing of nucleotides (He got Nobel prize
twice!)
Goldstein & Brown LDL receptor and its relation to familial hyper-
cholesterolemia
Griffith Transformation experiment
Jacob & Monad Operon model
James Lind Scurvy & citrus fruit trial in HMS Salisbury
Kary B Mullis Polymerase Chain Reaction
Kohler & Milstein Monoclonal antibodies by Hybridoma
technique
Linus Pauling & Robert
Corey
2o
structure of protein

The First in History
Genome to be sequenced Bacteriophage φX174
Genome that belongs to a free-living organ-
ism to be sequenced
H. Influenza
Sequence of human chromosome released Ch. 22
Protein to be sequenced (by sanger) ‘Bovine’ Insulin
Metabolic pathway discovered Glycolysis
Metabolic cycle discovered Urea Cycle
Disease treated by gene therapy ADA deficient SCID
Ribozyme discovered (by Cech) 26S rRNA
Molecular machine recognised Ribosome

Biochemical Tests
Test Detects
Gerhardt’s test, Rothera’s test Acetoacetate (ketone body)
Hay’s sulphur test Bile salts in urine
Fouchet’s test Bilirubin in urine (Qualitative test)
Ehrlich aldehyde test Urobilinogen
Vandenberg test Differentiates conjugated and
unconjugated bilirubin in serum
(Quantitative test)
Molisch test All carbohydrates
Benedict’s test All reducing substances (Reducing
sugar, Uric acid, Ascorbate etc.)
Barfoed’s test Monosaccharide
Seliwanoff’s test Fructose
Bial’s test Pentose sugars
Ninhydrin reaction Proteins with minimum of 2 peptide
bonds. (qualitative)
Biuret reaction Amino acids & proteins (Both Quali-
tative & quantitative)
Sakaguchi test Arginine
BCG dye binding method Albumin
Ferric chloride test Phenylketonuria, Tyrosinemia,
Alkaptonuria, MSUD
Alcian blue spot test Urinary glycosaminoglycans
Shake test (foam stability test) of
amniotic fluid
Fetal lung maturity assessment
Sulkowitch test Urinary Calcium

AIIMS May 2016
1. Which of the following is the second messenger for Nitric Oxide?
a. Ca2+
b. cAMP
c. cGMP d. Adenine
Ref : Harper 30th
ed., p.501; 660
Second messengers are diffusible, small molecules and are generated
intracellularly upon hormone (1st
messenger) binding to the membrane receptor.
They help in signal transduction from the receptor to the target.
First messenger 2nd
messenger Target of second messenger
Glucagon, Adrenaline cAMP Protein kinase A
NO, ANF (Atrial Na-
triuretic Factor)
cGMP Protein kinase G
Gastrin, ADH IP3
& Ca++
Protein Kinase C
Duration of action of second messenger is controlled by action of various reg-
ulating enzymes. For example, phosphodiesterase enzyme inactivates cAMP
by converting it to 5’AMP.
Significance of second messengers in hormonal action:
• Signal amplification: Second messengers amplify the signal produced
by first messengers
• Signal integration: 2nd
messengers can integrate information from
multiple independent upstream signals and there can be a cross-talk
between the second messenger pathways.
How to derive the answer?
Nitric Oxide & Natriuretic factors (ANP & BNP) are the only two first messen-
gers that use cGMP as the second messenger.
Option analysis:
Calcium is given to confuse those, who just had a glance on action of NO.
Extra Edge

ALA dehydratase forms porphobilinogen. As lead inhibits ALA dehydratase,
porphobilinogen level is not raised in urine in lead poisoning → option C is
AIIMS Nov. 2015
Topics asked in exam:
1. Heme biosynthesis
2. Plumboporphyria
3. Jaundice
4. Sickle cell Anemia – electrophoresis
5. Coenzyme role of Biotin
6. Coenzyme role of B12
7. Selenocysteine
8. Regulation of glycogen phosphorylase
9. Immune privileged site
10. Iron metabolism
11. Substrates for gluconeogenesis
12. Precipitation of proteins
13. Creatinine clearance
1. In lead poisoning which of the following is excreted in urine?
a. 𝛿 - ALA b. Urobilinogen
c. Porphobilinogen d. Glycine
Option analysis:
Glycine in urine:
• Glycinuria is an autosomal recessive disorder due to defective renal tubular
absorption of glycine.
• Associated with renal oxalate stones.
So, option D is ruled out.
Porphobilinogen in urine:
• ↑urinaryexcretionofporphobilinogenisseeninacuteintermittent porphyria

Chemistry of
Carbohydrates
1. Which of the following is not seen in human body?
a. L-fucose b. L-fructose
c. D-Glucose d. D- Fructose
2. All of the following are heteropolysaccharides, EXCEPT
a. Chitin b. Heparin
c. Hyaluronic acid d. Chondroitin sulfate
3. Which is the predominant monomeric unit of pectin?
a. Glucose b. Glucuronic acid
c. Galactose d. Galacturonic acid
4. Which of the following is a fructosan?
a. Pectin b. Chitin c. Inulin d. Glycogen
5. Which is the monomeric unit of lignin?
a. Glucose b. Fructose
c. Galactose d. Phenolic compound
6. Inositol is a
a. Nucleotide b. Polyhydroxy aldehyde
c. Polyhydroxy alcohol d. Polyhydroxy ketone
7. Sorbitol is a
a. Nitrate donor b. Polyhydroxy aldehyde
c. Polyhydroxy alcohol d. Polyhydroxy ketone
8. Correct statement about sucrose
a. Inert sugar
b. Reducing sugar
c. Made up of 13 carbons
d. α-D-glucopyranosyl-(1→2)-β-D-fructofuranoside
9. Alpha amylase acts on
a. α 1 → 4 bond b. α 1 → 6 bond
c. β 1→ 4 bond d. β 1 → 6 bond
10. Which of the following pentose sugar is present mainly in the heart
muscle?
a. Arabinose b. Lyxose
c. Xylose d. Xylulose
Answers are given in the printed version of the book in this place and
adequate explanations are given at the end of every chapter. Visit https://
www.aim4aiims.in/pg/buy-product.php?id=73 to get a printed copy.

Enzymology
1. All of the following are ribozymes, EXCEPT
a. snRNA b. rRNA
c. RNase H d. RNase P
2. All of the following are utilized by enzymes to reduce the activation
energy, EXCEPT
a. Entropy reduction
b. Desolvation of the active site
c. Conformational changes to the enzyme and substrate after interaction
d. Decrease in molecular collisions
3. The best measure of enzyme affinity is
a. Km b. Kd
c. Kcat d. Kcat/Km
4. The best measure of enzyme efficiency is:
a. Kcat b. Km
c. Km/Kcat d. Kcat/Km
5. All of the following forces are involved in Enzyme-Substrate complex
formation, EXCEPT
a. Covalent b. Electrostatic
c. Hydrogen d. Van der Waals
6. All of the following statements about enzymes are true EXCEPT:
a. Multienzyme complexes greatly reduce the rates of reactions
b. Isoenzymes differ in their amino acid sequence
c. Allosteric regulators usually do not bind to the active site of the enzyme
d. Transcriptional regulation is method of long term regulation of enzymatic
activity
7. Which of the following is the LEAST preferred method to separate
isoenzymes?
a. Agarose gel electrophoresis
b. Gel filtration chromatography
c. Ion-exchange chromatography
d. Affinity chromatography using the substrate as ligand
adequate explanations are given at the end of every chapter. Visithttps://
www.aim4aiims.in/pg/buy-product.php?id=73 to purchase the book.

Metabolism of
Carbohydrates
1. Which of the following is the flux generating enzyme of glycolysis?
a. Hexokinase b. Phosphofructokinase-1
c. Enolase d. Pyruvate kinase
2. Which of the following is the rate limiting enzyme of glycolysis?
a. Hexokinase b. Phosphofructokinase-1
c. Enolase d. Pyruvate kinase
e. Phosphofructokinase-1
3. All of the following are bifunctional enzymes, EXCEPT
a. Debranching enzyme b. PFK-1
c. PFK-2 d. Bisphospho glycerate mutase
4. Which of the following enzyme pair is involved in feedforward activation
of glycolysis?
a. Hexokinase & Enolase b. PFK-1 & Pyruvate kinase
c. PFK-1 & Enolase d. G3PDH & Pyruvate kinase
5. Which of the following enzymes is involved in both glycolysis and
gluconeogenesis?
a. Pyruvate kinase
b. Phosphofructokinase
c. Bisphospho glycerate kinase
d. Phosphoenolpyruvate carboxykinase
6. Which of the following enzymes is involved in both glycogen synthesis
and glycogenolysis?
a. Debranching enzyme
b. Debranching enzyme
c. Phosphohexose isomerase
d. Phosphoglucomutase
7. Which of the following is the negative homotropic allosteric modulator of
the enzyme PFK-1?
a. Citrate b. ATP
c. AMP d. ADP

Chemistry of Amino
Acids & Proteins
1. Which of the following amino acids is optically inactive?
a. Alanine b. Histidine
c. Threonine d. Glycine
2. Aminoacyl t-RNA is not directly required for the synthesis of
a. Proline b. Lysine
c. Hydroxy lysine d. Methionine
3. Which of the following amino acid has the most basic and positively
charged side chain?
a. Arginine b. Histidine
c. Lysine d. Cysteine
4. Isoelectric pH of lysine is calculated by taking the average of
a. pK1
and PK2
b. pK2
and PK3
c. pK1
and PK3
d. pK1
, PK2
and pK3
5. Alanine is similar to serine in the same way that
a. Val is similar to Thr b. Phe is similar to Tyr
c. Phe is similar to Trp d. Ser is similar to Thr
6. All of the following are dietary essential amino acids, EXCEPT
a. Methionine b. Lysine
c. Alanine d. Leucine
7. Which amino acid can form disulphide bonds?
a. Methionine b. Cysteine
c. Glutamate d. Glycine
8. The peptide bond has all the following characteristics EXCEPT that it is:
a. A partial double bond b. Covalent in nature
c. Free to rotate d. Planar in nature
9. Abnormal folding of proteins is responsible for the following disease:
a. Sickle cell anemia b. Prion disease
c. Nephrotic syndrome d. Hepatitis A

Metabolism of Amino
Acids
1. Which of the following is the storage form of proteins in human body?
a. Collagen b. Titin
c. Both d. None
2. To which of the following amino acids of target protein ubiquitin is
covalently added?
a. Glycine b. Valine c. Serine d. Lysine
3. What is the nature of bond between ubiquitin and the amino acid of the
target protein?
a. Glycosidic bond b. Hydrogen bond
c. Isopeptide bond d. Hydrophobic interaction
4. What is the minimum number of ubiquitin molecules that must be added
to a protein for its degradation in a proteasome?
a. 1 b. 3 c. 4 d. 6
5. Which of the following is NOT true about ubiquitin-proteasomal system?
a. Intracellular, short-lived regulatory proteins are degraded
b. Non-α peptide bond is formed by ubiquitin
c. Amino terminal Asp or Arg accelerate ubiquitination
d. ATP independent
6. Which of the following organ is the major source of alanine for liver in
between meals?
a. Muscle b. Brain
c. Kidney d. Adipocyte
7. In postprandial state, which of the following amino acid is extracted
predominantly by muscle, having been spared by the liver?
a. Alanine b. Valine
c. Glutamate d. Glutamine
8. Which is the only amino acid that undergoes significant amount of oxidative
deamination in the hepatic mitochondira?
a. Lysine b. Alanine
c. Threonine d. Glutamate

Heme Metabolism
1. Acquired porphyria is due to
a. Hg b. Pb c. Cu d. Sn
2. Lead inhibits
a. ALA dehydratase b. Ferrochelatase
c. Both d. None
3. Which of the following inborn error of metabolism can cause porphyria
like features?
a. Phenylketonuria b. Tyrosinemia type I
c. Alkaptonuria d. Metachromatic leukodystrophy
4. Biochemical basis of precipitation of porphyria by barbiturates is
a. Repression of ALA synthase
b. Derepression of ALA synthase
c. Rerepression of ALA synthase
d. miRNA mediated
5. Choluric jaundice is/are
a. Hepatic b. Post hepatic c. Both d. Hemolytic
6. Delta bilirubin is ______ bilirubin _____ bound to albumin.
a. Conjugated, covalently
b. unconjugated, non-covalently
c. Conjugated, noncovalently
d. unconjugated, covalently
7. Heme synthesis pathway operates in
a. Cytoplasm b. Mitochondria
c. Both d. None
8. Most common porphyria is due to deficiency of
a. PBG deaminase b. Uroporphyrinogen decarboxylase
c. Ferrochelatase d. Coproporphyrinogen oxidase
9. Bilirubin binding capacity of high-affinity site of serum albumin is
a. 15 mg bilirubin/100 ml of plasma
b. 25 mg bilirubin/100 ml of plasma
c. 35 mg bilirubin/100 ml of plasma
d. 45 mg bilirubin/100 ml of plasma

Lipid Chemistry and
Metabolism
1. Which of the following is a derived lipid?
a. Triacylglycerol b. Glycolipid
c. Lipoproteins d. Cholesterol
2. All of the following are prostanoids EXCEPT
a. Leukotrienes b. Prostaglandins
c. Prostacyclins d. Thromboxanes
3. All of the following are 18C unsaturated fatty acids except
a. Elaidic acid b. Linoleic acid
c. Oleic acid d. Stearic acid
4. All of the following are ω3
fatty acids EXCEPT
a. α-Linolenic acid b. Cervonic acid
c. γ-Linolenic acid d. Timnodonic acid
5. Which of the following is a tetraenoic acid?
a. Cervonic acid b. Timnodonic acid
c. Stearic acid d. Arachidonic acid
6. Arachidonic acid can be synthesised from
a. Linoleic acid b. α-Linolenic acid
c. Palmitic acid d. Stearic acid
7. Which of the following is NOT a membrane lipid?
a. Sphingomyelin b. Lecithin
c. Triacylglycerol d. Phosphatidylserine
8. Cephalin is
a. Phosphatidylethanolamine
b. Phosphatidylserine
c. Phosphatidylcholine
d. Phosphatidylglycerol
9. Which of the following phospholipid is found exclusively in mitochondrial
membrane?
a. Sphingomyelin
b. Phosphatidylethanolamine
c. Phosphatidylserine
d. Diphosphatidylglycerol

Nucleotide Chemistry &
Metabolism
1. Which of the following base is not found in DNA?
a. deoxy adenine b. deoxy guanine
c. deoxy cytidine d. Uracil
2. Which of the following purine is the most oxidised?
a. Adenine b. Hypoxanthine
c. Xanthine d. Uric acid
3. In deoxy adenosine monophosphate, phosphate group is esterified to
a. 2’ OH of ribose b. 3’ OH of ribose
c. 5’ OH of ribose d. None of the above
4. All of the following are correct statements regarding sources of purine
ring, EXCEPT
a. C2 is form formyl THFA
b. C4
, C5
& C7
are from Glycine
c. C6
is from respiratory CO2
d. N3
and N9
are from amide nitrogen of glutamine
5. Which is the end product of purine catabolism in non-primate mammals?
a. Allantoin b. Ammonia
c. Urea d. Uric acid
6. Which of the following condition causes hyperuricemia due to both
increased production and decreased excretion?
a. PRPP Synthetase over activity
b. Glucose-6-phosphatase Deficiency
c. Xanthine oxidase deficiency
d. Renal failure
7. Precursor of AMP and GMP is
a. IMP b. OMP c. TMP d. UMP
8. Which of the following is the substrate for the enzyme ribonucleotide
reductase?
a. Nucleoside monophosphate b. Nucleoside diphosphate
c. Nucleoside triphosphate d. All of the above

Free Radicals &
Antioxidants
1. All of the following are free radicals, EXCEPT
a. Superoxide b. Hydrogen peroxide
c. Hydroxyl radical d. Nitric oxide
2. All of the following are reactive oxygen species, EXCEPT
a. Superoxide b. Hydrogen peroxide
c. Hydroxyl radical d. Nitric oxide
3. Which of the following is produced when oxygen is reduced with 3
electrons?
a. Superoxide radical b. Hydrogen peroxide
c. Hydroxyl radical d. Water
4. The enzyme responsible for oxidative burst in neutrophils is
a. Catalase b. Myeloperoxidase
c. NADPH oxidase d. Superoxide dismutase
5. All of the following reactions are involved in generation of reactive oxygen
species within neutrophils for killing intracellular bacteria, EXCEPT
a. Superoxide dismutase reaction
b. Fenton’s reaction
c. NADPH oxidase reaction
d. Glutathione peroxidase reaction
6. All of the following are antioxidant enzymes, EXCEPT
a. Glutathione peroxidase
b. Glutathione reductase
c. Xanthine oxidase
d. Superoxide dismutase
7. Gene for which of the following antioxidant enzymes is mutated in Lou
Gehrig’s disease?
a. Superoxide dismutase b. Glutathione peroxidase
c. Glutathione reductase d. Catalase
8. Which one of the following is a chain-breaking antioxidant?
a. Glutathione peroxidase b. Selenium
c. Superoxide dismutase d. Catalase
9. Metal ion present in mitochondrial Superoxide dismutase is
a. Copper b. Iron
c. Manganese d. Molybdenum

Xenobiotics
Metabolism
1. Select the TRUE statement about biotransformation reactions
a. Detoxify the foreign compounds
b. Can convert a procarcinogen to carcinogen
c. Liver is the major site of biotransformation reactions
d. All of the above
2. Which of the following organelle is predominantly involved in phase I
detoxification of xenobiotics?
a. Golgi apparatus
b. Lysosome
c. Smooth endoplasmic reticulum
d. Rough endoplasmic reticulum
3. All of the following are true about adrenodoxin, EXCEPT
a. Adrenodoxin is a protein
b. Adrenodoxin contains heme
c. Found in the mitochondria of adrenal gland
d. Involved in steroid synthesis
4. All of the following are phase I biotransformation reactions, EXCEPT
a. Epoxidation b. Hydroxylation
c. Sulfation d. O-dealkylation
5. Which of the following molecule acts as a donor for sulfation reactions?
a. Cysteine
b. Methionine
c. Phospho adenosine phospho sulfate
d. Taurine
6. 450 in CYP450 denotes
a. 45% of cytochrome CYP1000
b. 450th
member in the family
c. Molecular weight is 450 kilodalton
d. Absorption peak at 450 nm
7. TRUE about CYP450 is
a. Monooxygenase b. Mixed function oxidase
c. Hydroxylase d. All of the above
Answers are given in the printed version of the book in this place and adequate
explanations are given at the end of every chapter. Visit https://

Molecular Biology
1. Human diploid genome consists of
a. 2 billion base pairs
b. 3 billion base pairs
c. 5 billion base pairs
d. 6 billion base pairs
2. Estimated number of human genes
a. 20 to 25 thousand b. 50 thousand
c. 60 thousand d. 1 lakh
3. How many genes are encoded by the human mitochondrial genome?
a. 37 b. 47
c. 57 d. 67
4. Deamination of ‘methylated cytosine’ will produce
a. Uracil b. Thymine
c. Hypoxanthine d. Adenine
5. Double stranded RNA exists in
a. A - DNA like conformation
b. B - DNA like conformation
c. Z - DNA like conformation
d. None
6. In mitochondrial genome, UGA codes for
a. Methionine b. N-formyl methionine
c. Tryptophan d. None
7. DNA gyrase is
a. Eukaryotic DNA topoisomerase I
b. Eukaryotic DNA topoisomerase II
c. Prokaryotic DNA topoisomerase I
d. Prokaryotic DNA topoisomerase II
8. Which of the following DNA polymerase is the most processive?
a. DNA Polymerase I b. DNA Polymerase II
c. DNA Polymerase III d. None
Answers are given in the printed version of the book in this place and adequate
explanations are given at the end of every chapter. Visit https://

Immunology
Biochemical basis of immunology is very important for PGI exams. Explaining the
answers for each question is beyond the scope of this book. The following questions are
very important for various exams.
1. The most efficient antigen presenting cell is
a. Macrophage b. B-cell
c. Natural killer cell d. Dendritic cell
2. All of the following are components of mononuclear phagocyte system,
EXCEPT
a. Endothelial cells
b. Mesangial cells in kidney
c. Kupffer cells in liver
d. Medullary macrophages in liver
3. Immunologically privileged site is
a. Area postrema b. Seminiferous tubule
c. Loop of Henle d. Optic disc
4. All of the following hypersensitivity reactions are humoral mediated,
EXCEPT
a. Type I b. Type II
c. Type III d. Type IV
5. C in CRP stands for
a. Choline of Corynebacterium
b. Concanavalin A
c. Capsular polysaccharide of pneumococci
d. Capsular polysaccharide of Corynebacterium
6. All of the following are negative acute phase proteins EXCEPT
a. Transferrin b. Albumin
c. Haptoglobin d. Transthyretin
7. Product of adenosine deaminase is
a. Xanthine b. Hypoxanthine
c. Inosine d. Adenosine monophosphate
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biochemistry/294306637648890

Cytoskeleton and Muscle
Biochemistry
1. Which of the following is a microfilament?
a. Actin b. Vimentin
c. Keratin d. Desmin
2. All of the following are cytoskeletal motors, EXCEPT
a. Dynein b. Actin
c. Myosin d. Dynamin
3. Which component of cytoskeleton is defective in Kartagener’s syndrome?
a. Dynein b. Actin c. Myosin d. Dynamin
4. Which component of cytoskeleton is defective in epidermolysis bullosa
simplex?
a. Desmin b. Vimentin
c. Keratin d. Dynamin
5. Hutchinson-Gilford progeria syndrome is due to mutation of
a. Keratin A b. Keratin B
c. Lamin A d. Lamin B
6. Calcium binding motif present in calmodulin is known as
a. Rossman fold b. EF hand
c. Zinc finger d. Actin fold
7. Sarcomere is a segment between
a. H and I bands b. Two I bands
c. Two Z disk d. None
8. TRUE statement about A-band:
a. Consists only of thin filaments
b. Contains the entire length of a single thick filament
c. I-band is a component of A-band
s. None
9. A single calmodulin polypeptide canbind to a maximum of
a. 2 calcium b. 3 calcium
c. 4 calcium d. 5 calcium

Nutrition
1. Calorific value of alcohol is
a. 4 Kcal/gm b. 5 Kcal/gm
c. 6 Kcal/gm d. 7 Kcal/gm
2. BMR is closely dependent on
a. Body surface area b. Lean body mass
c. BMI d. Height
3. Decreased BMR is seen in
a. Starvation b. Fever
c. Cold environment d. Cushing’s syndrome
4. Recommended Dietary allowance is calculated by
a. Estimated average intake + 2 Standard Deviation
b. Estimated average intake - 2 Standard Deviation
d. Estimated average intake ± 2 Standard Deviation
d. 2 X Estimated average intake
5. Steatorrhea is defined as stool fat exceeding
a. 7 gm per day b. 14 gm per day
c. 28 gm per day d. 32 gm per day
6. All of the following are components of Total Parenteral Nutrition, EXCEPT
a. Amino acids b. Fats c. Vitamins d. Fiber
7. Specific dynamic action is maximum for
a. Carbohydrates b. Proteins
c. Lipids d. Mixed diet
8. Which of the following fruit juice which helps in preventing urinary tract
infection?
a. Blueberry b. Cranberry c. Mulberry d. Raspberry
9.Whichofthefollowingphytochemicalisresponsibleforthecardioprotective
effects of red wine?
a. Sorbitol b. Resveratrol
c. Resorcinol d. Beta carotene

Image Based
Questions
1. What is the nature of the inhibitor shown in this Lineweaver-Burk plot?
a. Competitive b. Non-competitive
c. Uncompetitive d. Allosteric
2. What is the nature of the inhibitor shown in this Lineweaver-Burk plot?
a. Competitive b. Non-competitive
c. Uncompetitive d. Allosteric

Hemoglobin &
Myoglobin
1. Quaternary structure of Portland hemoglobin is
a. ζ2ϵ2 b. ζ2γ2
c. α2ϵ2 d. α2γ2
2. The shape of oxygen dissociation curve of myoglobin is
a. Parabola b. Hyperbola
c. Sigmoid d. Circular
3. Binding of carbon monoxide to iron of hemoglobin is unfavored because
of the steric hindrance provided by
a. Histidine E7 b. Histidine E8
c. Histidine F7 d. Histidine F8
4. How much oxygen can be carried by one deciliter of blood with 15 grams
of hemoglobin?
a. 7.5 mL of oxygen b. 15 mL of oxygen
c. 20 mL of oxygen d. 30 mL of oxygen
5. Increased oxygen affinity of fetal hemoglobin compared to HbA1 can be
explained by
a. α chain of fetal hemoglobin can’t bind to 2,3 BPG efficiently
b. α chain of fetal hemoglobin binds to 2,3 BPG more efficiently
c. γ chain of fetal hemoglobin binds to 2,3 BPG more efficiently
d. γ chain of fetal hemoglobin can’t bind to 2,3 BPG efficiently
6. Which of the following is the most common inherited single gene disorder
worldwide?
a. Thalassemia b. G6PD deficiency
c. Sickle cell anemia d. Pyruvate kinase deficiency
7. Cyanosis appears if reduced haemoglobin level is more than:
a. 5 g/dl b. 7 g/dl
c. 9 g/dl d. 10 g/dl
8. Carboxy hemoglobin is formed in the blood due to exposure to
a. CO b. CO2
c. O2
d. O3

Cell Membrane and
Transport
1. All of the following are components of eukaryotic cell membrane, EXCEPT
a. Triglycerides b. Carbohydrates
c. Lecithin d. Cholesterol
2. Which of the following has the lowest membrane permeability coefficient?
a. Na+
b. K+ c. Glucose d. Urea
3. A lipid bilayer is permeable to:
a. Urea b. Potassium
c. Glucose d. Sodium
4. How many amino acids are present in a single transmembrane alpha helical
region of a transmembrane protein?
a. 20 b. 30 c. 40 d. 50
5. Hydropathy plot values are helpful in recognizing the membrane spanning
regions of a proteins. Which of the following value in hydropathy plot can
suggest that hydrophobic sequence is a transmembrane segment?
a. >20 kcal/mol b. < 20 kcal/mol
c. >10 kcal/mol d. <10 kcal/mol
6. Glucose transporters (GLUT) are integral membrane proteins that traverses
the lipid bilayer several times. How many membrane spanning alpha
helices are present in GLUT proteins?
a. 1 b. 7 c. 10 d. 12
7. Glucose-6-phosphatase is a marker of
a. Plasma membrane b. Endoplasmic reticulum
c. Golgi apparatus d. Mitochondria
8. All of the following are markers of plasma membrane, EXCEPT
a. 5′-Nucleotidase b. Adenylyl cyclase
c. Adenylyl kinase d. Na+-K+-ATPase
9. All of the following post translational modification helps in anchoring of
proteins to the membrane, EXCEPT
a. Glycation b. Glypiation
c. Isoprenylation d. Myristoylation

PGI pattern questions for
practice
These questions are
exclusively given in this
ebook only.

PGI Pattern
1) Which of the following are post-translational modifications of
amino acyl residues of proteins?
a) Methylation
b) Formylation
c) Acetylation
d) Prenylation
e) Phosphorylation
2) Selenoproteins are
a) Selenoprotein P
b) Glutathione peroxidase
c) Glutathione reductase
d) Thioredoxin reductase
e) 5’ deiodinase
3) Hydrophobic amino acids are
a) Glycine
b) Alanine
c) Tyrosine
d) Asparagine
e) Proline
4) Non-protein amino acids are
a) L-Ornithine
b) L-Homocysteine
c) L- Diphthamide
d) L-Citrulline
e) L-Homo serine
5) Glutathione is made up of
a) Glycine
b) Lysine
c) Methionine
d) Cysteine
e) Glutamate
6) TRUE about molecular chaperones
a) Folding of all the proteins in the body require chaperones

b) Contain ATPase activity
c) Many of them are heat shock proteins
d) Bind to hydrophobic regions and prevent aggregation
e) Hsp 60 is a chaperonin
7) TRUE about prion proteins
a) PrPc is a glycoprotein rich in α helices
b) PrPc is a glycoprotein rich in beta sheets
c) PrPsc is rich in β sheet
d) PrPsc is rich in α helices
e) PrPsc acts as a template and is involved in the conversion of PrPc
to PrPsc
8) Select the TRUE statements
a) A linear tripeptide is linked by 3 peptide bonds
b) The C, N, O, and H atoms of a peptide bond are coplanar
c) Peptide bond is charged
d) Proline is a helix breaker
e) R group of tryptophan maximally absorbs light at 260 nm
9) Non-reducing sugars are
a) Glucose
b) Trehalose
c) Sucrose
d) Maltose
e) Galactose
10) Pentoses are
a) Arabinose
b) Xylose
c) Ribose
d) Xylulose
e) Erythrose
11) Carbohydrates found in glycoproteins are
a) N-Acetylglucosamine
b) N-acetylgalactosamine
c) Arabinose
d) L-Fucose
e) N-acetylneuraminic acid

12) Gluconeogenic substrates are
a) Lactose
b) Lactate
c) Pyruvate
d) Glycerol
e) Propionyl-CoA
13) Vitamin cofactors for PDH complex are
a) B1
b) B2
c) B3
d) B5
e) B6
14) Causes of non-ketotic hypoglycemia are
a) Diabetes mellitus
b) CPT I deficiency
c) Ingestion of unripe fruit of akee
d) Insulinoma
e) Type I Glycogen storage disease
15) Coenzyme A is made up of
a) Pantothenate
b) β mercaptoethylamine
C) Phospho ADP
d) Cobalamine
e) Biotin
16) Select the TRUE statements
a) Hepatocytes lacks thiophorase
b) Hepatocytes lacks Glucose-6-phosphatase
c) Humans lack L-Gulonolactone oxidase
d) Myocyte lacks Glucose-6-phosphatase
e) Humans lack cellulase
17) Irreversible steps of glycolysis are
a) Phosphorylation of glucose by hexokinase
b) Reaction by aldolase
c) Reaction by pyruvate kinase
d) Reaction by phosphoglycerate mutase

e) Reaction by Phosphofructokinase
18) Enzymes catalysing substrate level phosphorylation reactions are
a) Pyruvate Kinase
b) Phosphofructo kinase
c) Phosphoglycerate kinase
d) Glycerol kinase
e) Succinate thiokinase
19) Key enzymes of Gluconeogenesis are
a) Phosphoenol pyruvate carboxykinase
b) Fructose 1, 6 bisphosphatase
c) Pyruvate carboxylase
d) Glucose-6-phosphatase
e) Pyruvate kinase
20) High energy phosphate compounds are
a) Carbamoyl phosphate
b) Creatine phosphate
c) Glycerol-3-phosphate
d) 1,3-Bisphosphoglycerate
e) Phosphoenolpyruvate
21) All of the following are features of untreated type I GSD, EXCEPT
a) Lactic acidosis
b) Hyperlipidemia
c) Hyperuricemia
d) Raised bleeding time
e) Hypoglycemia
22) All of the following are features of untreated Galactosemia,
EXCEPT
a) Hypoglycemia
b) E. coli sepsis
c) Mental retardation
d) Jaundice
e) Premature ovarian failure
23) In which of the following conditions, non-essential amino acids
become dietarily essential?
a) Alkaptonuria

b) Maple syrup urine disease
c) Phenylketonuria
d) Homocystinuria
e) Hyperargininaemia
24) Hippuric acid is produced from the reaction of
a) Phenylacetate
b) Glycine
c) Glutamate
d) Propionyl CoA
e) Benzoyl CoA
25) Which of the following is/are derived from tryptophan?
a) Glutamine
b) Xanthurenic acid
c) Nicotinic acid
d) Urocanic acid
e) Kynurenine
26) Amino acids involved in the synthesis of beta hydroxy gamma
trimethyl ammonium butyrate are
a) Arginine
b) Leucine
c) Lysine
d) Serine
e) Methionine
27) Amino acids excreted in the urine in Cystinuria are
a) Cystine
b) Ornithine
c) Arginine
d) Lysine
e) Leucine
28) Which of the following amino acids does not undergo
transamination?
a) Lysine
b) Ornithine
c) Threonine
d) Proline

e) Hydroxyproline
29) All of the following enzymes are used in molecular techniques,
EXCEPT
a) Alkaline phosphatase
b) Polynucleotide kinase
c) Terminal transferase
d) RNAse H
e) DNA ligase
30) Which of the following cofactors are needed for the conversion of
phenylalanine to adrenaline?
a) Tetrahydrobiopterin
b) Vitamin C
c) Copper
d) Vitamin B6
e) S-Adenosyl methionine
31) Vitamin C is NOT required for
a) Carnitine biosynthesis
b) Creatine biosynthesis
c) Collagen maturation
d) Iron absorption
e) Regeneration of tocopherol
32) Factors increasing iron absorption are
a) Acidic pH
b) Tannin
c) Phytate
d) Ascorbate
e) Oxalate
33) Divalent Metal Ion transporter-1 is involved in the transport of
a) Fe2+
b) Mg2+
c) Fe3+
d) Cu+
e) Pb2+
34) Cardiac enzymes are ….
a) CK-MB

b) LDH
c) SGOT
d) SGPT
e) Troponin
35) Trinucleotide repeat disorders are
a) Alzheimer’s disease
b) Amyotrophic lateral sclerosis
c) Ataxia telangiectasia
d) Huntington’s chorea
e) Kennedy’s disease
36) True statement(s) about reverse transcriptase
a) Used in cDNA synthesis
b) RNA dependent DNA polymerase predominantly
c) DNA dependent DNA polymerase predominantly
d) Telomere is an example
e) Used by HIV
37) What are all the features of polymerase used in PCR
a) Thermostable
b) 5’  3’ polymerase activity
c) Requires primer
d) 5’  3’ exonuclease activity
e) 3’  5’ exonuclease activity
38) B12 dependent enzymes present in human are
a) Methionine synthase
b) Methyl malonyl coA mutase
c) Lysine amino mutase
d) Leucine aminomutase
e) Cystathionine synthase
39) B1 dependent enzymes are
a) Pyruvate Dehydrogenase
b) α keto glutarate dehydrogenase
c) Branched chain keto acid dehydrogenase
d) Transketolase
e) Transaldolase
40) Biotin dependent enzymes are

a) Acetyl CoA carboxylase
b) Pyruvate carboxylase
c) Propionyl CoA carboxylase
d) Vitamin K dependent carboxylase
e) Methylcrotonyl-CoA carboxylase
41) Raised anion gap is seen in
a) Multiple myeloma
b) Lithium poisoning
c) Uremia
d) Aspirin poisoning
e) Lactic acidosis type I
42) In glycoproteins, sugar residues are added to the
a) OH group of serine
b) OH group of threonine
c) OH group of tyrosine
d) Amide nitrogen of asparagine
e) Amide nitrogen of glutamine
43) GPI linked proteins are
a) Acetylcholinesterase of red cell membrane
b) Placental and intestinal alkaline phosphatase
c) 5′-Nucleotidase
d) Decay-accelerating factor
e) Adenylyl cyclase
44) FAD acts as a coenzyme for
a) Succinate dehydrogenase
b) Acyl CoA dehydrogenase
c) Malate dehydrogenase
d) Mitochondrial Glycerol-3-phosphate dehydrogenase
e) Glutathione peroxidase
45) Markers of plasma membrane are
a) Adenylate kinase
b) Adenylyl cyclase
c) Na+K+ATPase
d) 5’ Nucleotidase
e) 5’ deiodinase

46) Oncogenes are
a) RAS
b) MYC
c) HER2
d) BCL2
e) BID
47) TRUE about mitochondrial DNA
a) Contains 37 genes
b) Maternally inherited
c) Genetic code of mitochondira is different
d) Mitochondrial genome is polyploid
e) Circular & double stranded
48) Select the TRUE statement(s) regarding ADP-ribosylation
a) Pertussis toxin causes ADP-ribosylation of α subunit of Gi type
of G-protein
b) Cholera toxin causes ADP-ribosylation of α subunit of Gs type
of G-protein
c) ADP-ribosylation of EF-2 is done by diphtheria toxin
d) ADP-ribosylation of histones is associated with DNA repair
e) ATP is the source of ADP-ribose
49) NADP act as a coenzyme for
a) Glucose-6-Phosphate dehydrogenase
b) Malic enzyme
c) Malate dehydrogenase
d) Cytosolic isocitrate dehydrogenase
e) Acyl coA dehydrogenase
50) TRUE about micro RNA
a) transcribed by RNA polymerase II
b) 200 nucleotides in length
c) Primary miRNA contains 5’ cap and a 3’ polyadenylated tail
d) translocated to cytoplasm by exportin-5
e) miRNA base pair with 5’ untranslated region of target mRNA
51) TRUE amount complement system
a) C3b & C4b are opsonins
b) C3a, C4a, C5a are anaphylatoxins

c) C5b678(9)n forms membrane attack complex
d) Early complement component deficiency leads to autoimmune
diseases
e) Late complement component deficiency leads to pyogenic
infections
52) TRUE about dendritic cells
a) Dendritic cells are the most efficient professional antigen
presenting cells
b) constitutively express MHC II and co-stimulatory signal
molecule B7
c) can activate naïve T-cell.
d) produce cytokines
e) present in skin
53) ABC transporters are involved in
a) Intestinal absorption of copper
b) Biliary excretion of copper
c) Methotrexate resistance
d) Reverse cholesterol transport
e) Chloride transport
54) Select the wrong statement(s)
a) DNA is more stable
b) DNAse is more stable
c) RNA is more stable
d) RNAse is more stable
e) Both DNAse & RNAse are equally stable
55) Disorders of ubiquitin proteasomal system are
a) Angelman syndrome
b) Autosomal recessive juvenile Parkinson’s disease
c) Von Hippel-Lindau syndrome
d) Congenital polycythaemia
e) Sickle cell anemia
56) ω-3 fatty acids are
a) Linoleic acid
b) Alpha Linolenic acid
c) Gamma linolenic acid

d) Docosahexaenoic Acid (DHA)
e) Eicosapentaenoic acid (EPA)
57) 18 carbon fatty acids are
a) Arachidonic acid
b) Linoleic acid
c) Oleic acid
d) Palmitic acid
e) Stearic acid
58) Lipotropic factors are
a) Choline
b) Methionine
c) Betaine
d) Selenium
e) Vitamin E
59) Reactions taking place inside the mitochondria are
a) TCA cycle
b) Omega oxidation of fatty acids
c) Elongation of long chain fatty acids
d) Ketone body production
e) Part of gluconeogenesis
60) Sulphur containing amino acids are
a) Methionine
b) Cysteine
c) Homocysteine
d) Taurine
e) Serine
61) Sulphur containing amino acids found in proteins are
a) Methionine
b) Cysteine
c) Homocysteine
d) Taurine
e) Serine
62) Compounds with free sulfhydryl group are
a) Cysteine
b) Cystine

c) Methionine
d) Glutathione
e) Coenzyme A
63) Hemoproteins are
a) Catalase
b) Guanylyl cyclase
c) Tryptophan pyrrolase
d) Cytochrome C oxidase
e) Myoglobin
64) Which is/are NOT true about collagen?
a) Collagen helix is a right handed alpha helix
b) Tertiary structure of collagen is left-handed triple helix
c) Triple helix structure is formed intracellularly
d) Self-assembly is the cardinal principle in collagen maturation
e) Hydroxy proline residues are glycosylated
65) Select the true statement (s):
a) Zinc is involved in the storage of insulin
b) Calcium is involved in insulin release
c) Chromium is an insulin sensitizer
d) Insulin inhibits Lipoprotein lipase
e) Insulin causes intracellular shift of potassium
66) All are true regarding tRNA EXCEPT
a) 74 to 95 nucleotides long
b) There are at least 20 species of tRNA molecules in every cell
c) Do not undergo any processing like mRNA
d) 5’ end of tRNA contains CCA
e) Transcribed by RNA polymerase II
67) All are true about microsatellite repeats EXCEPT
a) consist of 2 to 6 nucleotides repeated up to 50 times
b) Repeats of 2 nucleotides (dinucleotide repeats) is the most
common form of microsatellite.
c) Highly polymorphic
d) Co-dominantly inherited
e) Multi-allelic

68) Which of the following pair of gene and its chromosomal location
is INCORRECT?
a) RB – 13
b) CFTR – 7
c) MHC I – 6
d) TP53 – 17
e) WT1 – 11
69) All of the following are disorders with X-linked dominant
inheritance, EXCEPT
a) Vit D dependent rickets
b) Rett syndrome
c) Incontinentia pigmenti
d) Fragile-X-Syndrome
e) Most cases of Alport syndrome
70) Enzymes coded by the X-chromosomes are
a) Uroporphyrinogen III synthase
b) α-Galactosidase
c) Arylsulfatase A
d) Iduronate sulfatase
e) α-L-Iduronidase
71) Ribozymes are
a) Peptidyl transferase
b) Telomerase
c) Spliceosomes
d) RNAse H
e) Reverse transcriptase
72) Prokaryotic DNA polymerase I contain
a) 5'3' polymerase activity
b) 3'5' polymerase activity
c) 3'5' exonuclease activity
d) 5'3' exonuclease activity
e) 5'3' endonuclease activity
73) Inhibitors of translation only in eukaryotic organisms are
a) Cycloheximide
b) Ricin

c) Diphtheria toxin
d) Puromycin
e) Linezolid
74) Components of Garrod’s tetrad are
a) Phenylketonuria
b) Alkaptonuria
c) Albinism
d) Cystinuria
e) Essential Pentosuria
75) Proteins and enzymes involved in reverse cholesterol transport are
a) ABCA1
b) ABCG1
c) LCAT
d) CETP
e) SRB1
76) Hypouricemia is due to
a) Overactivity of xanthine oxidase
b) Defective xanthine oxidase
c) Renal failure
d) Liver failure
e) Defective HGPRTase
77) Orotic aciduria is seen in
a) Rye syndrome
b) Orotidylate decarboxylase deficiency
c) Ornithine transcarbamoylase deficiency
d) Allopurinol therapy
e) 6-Azauridine therapy
78) Products of RNA polymerase III are
a) tRNA
b) 5S rRNA
c) U6 SnRNA
d) miRNA
e) 7S RNA of signal recognition particle
79) Properties of genetic code are
a) Degenerate

b) Overlapping
c) Universal
d) Unambiguous
e) Punctuated
80) Non-coding RNAs are
a) tRNA
b) miRNA
c) rRNA
d) long non-coding RNA
e) snRNA
81) TRUE about restriction enzymes
a) can cut the DNA anywhere
b) produce only sticky ends
c) produce only blunt ends
d) produced by bacteria against viruses
e) can cleave single stranded DNA
82) TRUE about lipid rafts
a) specialised areas in the inner layer of the lipid bilayer
b) specialised areas in the outer layer of the lipid bilayer
c) involved in signal transduction
d) enriched in cholesterol and sphingolipids
e) caveolae are derived from lipid raft
83) Hormones that bind to intracellular receptors are
a) calcitonin
b) Calcitriol
c) Thyroxin
d) Progestins
e) Retinoic acid
84) β alanine is present in
a) Coenzyme A
b) Carnosine
c) Anserine
d) Homocarnosine
e) Sarcosine

85) Amino acids containing polar, uncharged side chains are
a) Asparagine
b) Serine
c) Tyrosine
d) Cysteine
e) Glutamine
86) Enzyme markers of obstructive liver disease are
a) Alkaline phosphatase
b) Aspartate transaminase
c) Lactate dehydrogenase
d) 5’-Nucleotidase
e) Gamma glutamyl transpeptidase
87) Laboratory findings seen in prehepatic jaundice due to
intravascular hemolysis are
a) ↑ LDH
b) ↑ urinary urobilinogen
c) ↑ urinary bilirubin
d) ↓ Hemopexin
e) ↓ Haptoglobin
88) ApoB B100 containing lipoproteins are
a) Chylomicron
b) VLDL
c) IDL
d) LDL
e) HDL
89) Enzymes that belong to EC4 are
a) Enolase
b) Aldolase
c) Fumarase
d) ALA dehydratase
e) Thiophorase
90) Copper containing enzymes are
a) Glutathione peroxidase
b) Lysyl oxidase
c) Cytochrome c oxidase
d) Tyrosinase
e) Alkaline phosphatase
91) Anti-oxidant vitamins are

a) Beta carotene
b) Ascorbic acid
c) Tocopherol
d) Calcitriol
e) Menaquinone
92) Reactions producing H2O2 are
a) Xanthine oxidase
b) Superoxide dismutase
c) L-amino acid oxidase
d) D-amino acid oxidase
e) Cytochrome C oxidase
93) Techniques to quantify the gene expression are
a) Quantitative real-time PCR
b) Flowcytometry
c) Fluorescence In Situ Hybridization
d) RNA microarray
e) SDS-PAGE
94) Techniques to detect DNA-Protein interaction are
a) South-western blotting
b) SDS-PAGE
c) DNA finger printing
d) DNA foot printing
e) Chromatin immunoprecipitation
95) Isoprene derivatives are
a) Cholesterol
b) Ubiquitin
c) Ubiquinone
d) Dolichol
e) β-carotene
96) Food additives that prevent lipid peroxidation are
a) Propyl gallate
b) Butylated hydroxyanisole
c) Butylated hydroxytoluene
d) Tocopherol
e) Calcitriol
97) In our body, chemical reactions which are thermodynamically not
possible (endergonic reactions) are made possible by coupling with

exergonic reactions. In all of the following reactions 2 high energy
phosphates are used in coupling, EXCEPT
a) Activation of fatty acid for beta oxidation
b) Activation of amino acid for charging into tRNA
c) Activation of ubiquitin for tagging into target protein
d) Activation of glycerol for TAG synthesis.
e) Activation of glucose for glycolysis
98) Immunological tolerance can be induced by
a) High doses of antigen
b) Intravenous or oral introduction
c) Absence of adjuvants
d) Low levels of co-stimulation
e) Presentation of antigen by immature or non-activated antigen-
presenting cells
99) Amino acids that donate one carbon group are
a) Glycine
b) Serine
c) Methionine
d) Histidine
e) Threonine
100) Glutathione is involved in
a) Meister cycle
b) Conjugation of xenobiotics
c) Free radical scavenging
d) Leukotriene synthesis
e) Maleylacetoacetate cis, trans isomerase reaction
101) True about trans fatty acid
a) high in fried rice
b) partial hydrogenation increase it
c) refining decrease it
d) increased LDL
e) increased HDL
102) Sphingosine is synthesised from
a) Glycine
b) Serine
c) Mannose 6 phosphate
d) Propionyl coA
103) Gangliosides contain

a) Phosphate
b) Galactose
c) Sulfate
d) Serine
e) Sialic acid
104) Neuraminic acid is derived from
a) Pyruvate
b) Mannosamine
c) Propionyl coA
d) Lysine
e) Methionine
All these questions are framed from
the content given in the printed
book.
So, there will be no problem in
answering the questions.

Aim4 aiims biochemistry-free-sample

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