NEET 2020 Recall
Questions
Q1. During low insulin-glucagon ratio, which of the following will be
active ?
a)G-6-phosphatase
b)Phospho fructo kinase
c)Glucokinase
d)Hexokinase
• Low insulin glucagon ratio means it is fasting state, as in fed state
insulin is more. So in fasting state glucose-6-phosphatase will be
active as this enzyme is involved in gluconeogenesis, which occurs
during fasting.
• Phospho fructo kinase is involved in glycolysis. PFK-1 is active in any
situation and PFK-2 is active only in fed state.
• Glucokinase phosphorylates glucose in liver and pancreas, active in
fed state and is induced by insulin.
• Hexokinase also phosphorylates glucose and is present in all cells of
the body. It is active in any situation in body as it is a general enzyme
to phosphorylate glucose.
• Video: Gluconeogenesis
(Unit III : Carbohydrate Metabolism)
• Notes: Page 41
Q 2. Apo- B48 made by?
a) RNA splicing
b) RNA editing
c) RNA interference
d) DNA translocation
• In liver cell, Apo B 100 gene gives rise to Apo B 100 protein.
• But Apo B 48 protein is made in intestinal cells from the gene encoding
Apo B 100, by the process of RNA editing, which is also known as
Differential RNA processing or chemical modification of RNA. This is a
post transcriptional modification.
• RNA splicing is also a post transcriptional modification but this is removal
of introns.
• RNA interference is silencing technique where the gene is silenced by not
letting the product of gene formed.
• Translocation occurs during translation. This is movement of ribosome over
mRNA.
• Video: Transcription
Unit VII: Molecular Biology
• Notes: Page140
Q3. If alanine is replaced by _______ , absorption at 280 nm will
increase.
a)Tryptophan
b)Lysine
c)Leucine
d)Proline
• Proteins and amino acids absorb UV-light at 280 nm, due to aromatic
nature of these amino acids &they have conjugated double bonds in
the rings. Maximum absorption occurs by tryptophan as it has 2 rings
in its side chain.
• Unit V : Amino acids and Proteins ; Video: Classification and Metabolism of Amino acids
• Conceptual Review of Biochemistry : By Smily Pruthi Pahwa (Page 282).
Q 4: Thymine is 28% in DNA, What is the percentage of cytosine?
a)28%
b)44%
c)22%
d)72%
• Cytosine-22%
By chargaff’s rule, number of purines equal the number of pyrimidines
in a double stranded DNA
• So, amount of Adenine = Thymine, as they pair with each other by two
hydrogen bonds. As thymine given is 28 %, so total A+T is 56%.
• Now also, amount of Guanine = Cytosine, as they pair with each other
by three hydrogen bonds.
Remaining 44% equally distributed in 22% each for guanine and
cytosine.
• Question bank (MCQs): Biochemistry
• Unit VII: Molecular Biology
• Video: Basics of Genetics
• Notes: (Page 129)
Q5: Nitric oxide is produced from which amino acid?
a)Arginine
b)Aspartate
c)Proline
d) Glycine
• NO is also called as Endothelium Derived Relaxing Factor (EDRF).
• NO (nitric oxide) is synthesized from arginine by enzyme NOS (Nitric
oxide synthase) in the endothelial cells.
• The vasodilator – nitroglycerin also enters smooth muscle cells, where its
metabolism also leads to the formation of NO.
• There are three isoforms of NOS (Nitric oxide synthase)
a. nNOS - neuronal
b. iNOS- inducible
c. eNOS- endothelial
• Conceptual Review of Biochemistry : By Smily Pruthi Pahwa
(Page No:189)
Q6. A 21 years old male patient has pain in joints. Patients’s urine
sample was collected turned black on exposure to air. Name the
enzyme which is deficient?
a) OTC (ornithine trans carbamoylase)
b) Orotic Acid
c) Homogentisate Dioxygenase
d) Phenyl alanine oxidase
• Diagnosis is alkaptonuria. Urine turns black on exposure to air due to
oxidation of homogentisic acid. Enzyme deficient is homogentisate
dioxygenase or homogentisate oxidase.
• Video: Phenylalanine and Tyrosine Metabolism
• Unit V: Amino acids and Proteins.
• Notes: Page 78
• Rapid Revision : Page no: 25
Q7. In non competitive inhibition, what is change of Km and Vmax?
a)Km decrease
b)Km increase
c)Vmax no change
d)Vmax decrease
In Non-Competitive Inhibition: Inhibitor binds at regulatory site of
the enzyme and induces changes in the active site so that substrate
cannot bind and thus decreases the velocity of the reaction. But there
is no change in Km or Substrate concentration.
Km is increased in case of competitive inhibition, where the inhibitor
binds at the active site.
• Enzymology: Unit IV
• Video Enzyme Inhibitors
• Rapid Revision : Page no: 38
• Notes: Page 61
Q8: During warfarin therapy, which of the following factor is reduced
in blood ?
a) Factor 2
b) Factor 11
c) Factor 5
d) Tissue factor
Warfarin is a competitive inhibitor of vitamin K, which is important for clotting factors
2,7,9 & 10
• Vitamin K video
• Unit VIII: Miscellaneous
• Rapid Revision (Page no: 67)
• Notes: Page 188
Q9:Which proteoglycan is present in glomerular basement membrane ?
a) ChondroitinSulphate
b) HeparanSulphate
c) KeratanSulfate 1
d) KeratanSulfate 2
• Heparan sulfate is present in basement membrane of glomerulus. Also,
it is present on cell surfaces and has a role in retinal cell-cell
attachment.
• Classification of Carbohydrate video:
• Unit II: Carbohydrate Chemistry
• Conceptual Review of Biochemistry : By Smily Pruthi Pahwa: (Page 39)
Q10: Inheritance in Marfan’s syndrome?
a) AD
b) AR
c) X-linked recessive
d) X-linked dominant
• Inheritance in Marfan’s Syndrome is Autosomal Dominant
• Mutation in gene for Fibrillin-I.
• Clinical Features: Tall structure, long arms and legs, loose joints, lens
dislocation, rupture aorta.
• Video: Fibrous Proteins
• Unit V: Amino Acid and Proteins
• Conceptual Review of Biochemistry : By Smily Pruthi Pahwa: (Page 305)
Q11. Which of the following is true about protein structures:
a) 2° structure is stabilized by disulfide bond
b) 1°,2° & 3° structures can be destroyed by denaturation
c) 2°& 3° structures are based on amino acid sequence
d) secondary structure is the three dimensional structure of protein
Ans:
• Disulfide bond is not present in 2° structure, but is present in tertiary structure.
• 1 ° structure is not destroyed by denaturation.
• 2 ° & 3° structures are based on amino acid sequence, Infact the overall
protein structure depends upon amino acid sequence. Even change of one
amino acid can affect the overall structure & function of protein.
• Secondary structure is not the three dimensional structure of protein. The
overall three dimensional structure of a polypeptide is called its tertiary
structure.
• Tertiary structure is due to overall interactions between the R groups of
amino acids. Secondary structure is due to local interactions between
stretches of a polypeptide chain.
• Video: Protein Bonds and Structure (Unit V: Amino acids and Proteins)
• Rapid Revision (Page no:49)
• Notes: Page 95
Evidence based Summary
• Total ques ons: 11
• Rapid Revision:4
• Ques on from Medical PG/FMGE videos: 10
