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Biochemistry: Topic-Wise Questions
Biochemistry: Topic-Wise Questions
Topic-wise Questions
1.
The graph given below denotes the transport 3. Michaelis Menten curve below characterizes an
kinetics across the cell membrane. The solute is allosteric enzyme system. True statement is
[AIIMS May 2016] [AIIMS May 2016]
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a. Modifier at the allosteric site can affect the
catalytic site too
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2.
Graph shown below is the titration curve of a 4. Which one of the following statements is TRUE
Ans. biochemical compound. Which of the following regarding this image which depicts the effect of an
1. c statement is true? [AIIMS May 2016] inhibitor on the velocity of enzyme action?
2. b [Recent Question 2016]
3. a
4. d
BIOCHEMISTRY
5. Contribution of Scientists (Photograph) in Field of 8. Source of the Substance (Photograph) in Urine is
Biochemistry [Recent Question 2012]
a. Arginase
b. Glutaminase
a. Synthesis of Gene c. Glutamate dehydrogenase
b. Extraction of Enzyme d. Urease
c. DNA as a genetic material
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d. Structure of DNA
9. Identify the Type of transport mechanism ‘B’ as
6. Type of Collagen found in Membrane (Arrow) in
Photograph [Recent Question 2014]
,3 shown in Photograph
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Ph
a. Uniport b. Symport
a. Type I b. Type II
c. Type III d. Type IV
c. Antiport d. Exocytosis Ans.
5. d
6. d
7. Most common type of Protein (Photograph) found 10. Folds in Molecule shown in the Photograph is due 7. a
8. b
in Human body [Recent Question 2012] to [Recent Question 2012]
9. b
10. a
11. Glucose in transported in Organ (Box) shown in 14. Type of reaction shown in the Photograph is
Photograph via [Recent Question 2013]
a. Oxidative reaction
b. Reduction reaction
c. Hydrolysis
a. GLUT 1 b. GLUT 2 d. Sulfur conjugation
c. GLUT 3 d. GLUT 4
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12.
Reaction NOT seen in Organelle shown in 15. Identify the Transport mechanism shown in the
Photograph [Recent Question 2012] Photograph
,3 [Recent Question 2016]
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Ph
BIOCHEMISTRY
Figure B1 (17-24)
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17. Enzyme of Pathway (Figure B1) common to Gluco- 21. Dead-end metabolite in Pathway shown (Figure
neogenesis [Recent Question 2014] B1) is [Recent Question 2014]
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Figure B2 (25-30)
PHOTON 20
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25. NOT a Key enzyme of Pathway shown (Figure B2) 28. Activation of pathway shown (Figure B2) is done by
Ph
BIOCHEMISTRY
31. Epimers of Sugar shown in Photograph include 32. Intermediate of Glycolysis shown in Photograph
[Recent Question 2012] occur in [Recent Question 2013]
Figure B3 (33-38)
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Ph
Ans.
31. c
32. b
33. b
33. Pathway shown in the Photograph produces 36. True statement regarding pathway shown in Figure 34. a
[Recent Question 2014] B3 35. d
a. ATP b. NADPH a. ATP utilised b. ATP produced 36. d
c. ADP d. Acetyl CoA c. ATP both utilized and produced 37. c
34.
Rate limiting step of Pathway (Figure B3) is d. ATP neither utilized nor produced 38. d
catalyzed by 37. Significance of pathway shown in Figure B3 include
a. Glucose-6-phosphatase dehydrogenase all EXCEPT
b. Gluconolactone hydrolase a. Free radical scavenging
c. 6-phospho-gluconate dehydrogenase b. RBC membrane integrity
d. Transketolase c. Energy production
35. Pathway shown in Figure B3 is seen in the following d. Generation of reducing equivalents
organ(s) 38. True regarding pathway shown in Figure B3
a. Liver a. Glucose shunted through this pathway
b. Adipose tissue b. Monophosphates only as intermediates
c. Adrenal cortex c. Direct oxidative pathway of glucose metabolism
d. All of the above d. All of the above
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•• Midpoint: When the number of moles of strong base added to similar structural configuration of both Inhibitor and
equals half of the moles of weak acid already present; thus, Normal substrate
the midpoint is half of the equivalence point
At midpoint, pH = pKa
,3 Competitive inhibition can be reversed or relieved by
increasing substrate concentration
Buffering capacity is maximum
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Kinetics: Km is increased, Vmax remains unchanged
•• Non-Competitive Inhibitor
Inhibitor is different from substrate: Binds to enzyme at a
on
Topper’s edge..................................................
COLLAGEN
•• Uncompetitive Inhibitor
Bind to Enzyme-Substrate (ES) complex to form ESI
•• The curve starts at a higher pH than a titration curve of a (Enzyme Substrate Inhibitor) complex: Binding occur at a
site distant or overlapping with active site
strong base
Kinetics: Decreased Vmax, Decreased Km
•• There is a steep climb in pH before the first midpoint
•• Gradual increase of pH until past the midpoint.
•• Right before the equivalence point there is a sharp increase
5. Ans. (d) Structure of DNA
in pH [Ref. Chatterjee, 8/e p250; Vasudevan, 6/e p470]
•• pH steadies itself around the midpoint because the solutions
WATSON & CRICK (PHOTOGRAPH) MODEL OF DNA
at this point in the curve are buffer solutions, which means
•• Right handed double helix
that adding small increments of a strong base will only
•• Complimentary strands
barely change the pH
•• Antiparallel strands
•• Increase in pH near the equivalence point
•• Hydrogen bonds between bases
•• Number of equivalence points determine the number of •• Chargaff rule: A pairs with T, G pairs with C
ionisable groups; So here toe ionisable groups are there •• Helix 20 Å diameter
•• Zone between the two equivalence points is region of •• Pitch of spiral: 3.4 nm per turn
buffering as there is slow rise or resistance to change in pH •• 10 base pairs within each turn
Answers & Explanations 121
•• Hydrolytic release of the amide nitrogen of glutamine as
BIOCHEMISTRY
Topper’s edge.................................................. ammonia (Photograph), catalysed by glutaminase, strongly
favours glutamate formation
•• DNA replication: Watson and Crick model suggests that •• An analogous reaction is catalysed by L –asparaginase
because one strand of DNA is the complement of the other,
•• Concerted action of glutamine synthetase and glutaminase
upon unwinding of the double helix (dsDNA), each strand
(ssDNA) acts as a template for the formation of a new strand
thus catalyses the interconversion of free ammonium ion
and glutamine
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•• Type III: Skin, Lungs, Vascular tissues 10. Ans. (a) Glycine
•• Type IV: Basement membranes
[Ref. Harper, 30/e p628]
COLLAGEN
•• Structural composition: Glycine (33%), Proline (10%),
8. Ans. (b) Glutaminase Hydroxyproline (10%) and Hydroxylysine (1%)
[Ref. Harper, 28/e p495] •• Has a triple helical structure
•• Lysine residues form intramolecular covalent cross links
•• Intermolecular covalent cross-links are formed by two
hydroxylysine residues along with one lysine residue
•• Glycine residues at every third position of the triple helical
portion of the alpha chain
•• Repeating structure, represented bas (Gly-X-Y)n, is an
absolute requirement for the formation of the triple helix
(where X and Y can be any other amino acids)
•• GLUT 5: Small intestine Absorption of fructose •• Pinocytosis: A form of endocytosis in which small particles
PHOTON 20
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Gluconeogenesis Cytosol + mitochondria
Krebs (TCA) cycle Mitochondria
ETC Mitochondria ,3 Topper’s edge..................................................
•• A in Photograph: Uniport moves one type of molecule in a
13. Ans. (b) Gene synthesis bidirectional manner
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•• C in Photograph: Antiport moves two molecules in opposite
[Ref. Biochemistry by Chakravorty, 1/e p272] directions (e.g.: Na+ - K+ pump)
DR HARGOBIND KHORANA (PHOTOGRAPH)
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•• First synthetic gene available was a yeast tRNA synthesized 17. Ans. (d) Phosphoglycerate kinase
by Dr Hargobind Khorana in 1972
•• Nobel prize winner [Ref. Harper, 26/e p136, 210]
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18. Ans. (c) 2-carbon end-product is formed •• Committed step, irreversible step and bottle neck of
BIOCHEMISTRY
glycolysis
[Ref. Harper, 26/e p136]
•• Aerobic glycolysis produces 8 moles of ATP per mole 25. Ans. (c) Pyruvate kinase
of glucose and a 3 carbon compound pyruvate is the end [Ref. Harper, 26/e p153]
product
•• Anerobic glycolysis (Photograph) produces 2 moles of ATP
KEY ENZYMES OF GLUCONEOGENESIS (PHOTOGRAPH)
per mole of glucose and a 3 carbon compound lactate is the Pyruvate Mitochondrial origin
end product carboxykinase Catalyzes conversion of pyruvate to OAA
•• This whole chain of reactions is not a complete breakdown Malate shuttle transfers OAA into cytosol
of glucose as the end product pyruvate enters mitochondria PEP Cytosol in origin
for further break down carboxykinase Catalyzes conversion of OAA to
phosphoenolpyruvate
19. Ans. (c) Glyceraldehyde-3-phosphate dehydrogenase Fructose-1,6- Cytosol in origin
[Ref. Harper, 26/e p136] bisphosphatase Reversal of the PFK action.
Glucose-6- Cytosol in origin
STEP 6 OF GLYCOLYSIS (PHOTOGRAPH)
phosphatase Reversal of the hexokinase/glucokinase
•• Enzyme: Glyceraldehyde-3-phosphate dehydrogenase action
•• Conversion of G-3-P to high energy compound 1,3-
bisphospho glycerate
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26. Ans. (c) Partial Mitochondrion, partly Cytoplasm
•• Inorganic phosphate is utilized and NADH is generated
[Ref. Harper, 26/e p153]
20. Ans. (b) 1 cycle produce 2 ATPs
[Ref. Harper, 26/e p136]
,3 GLUCONEOGENESIS (PHOTOGRAPH)
•• Responsible for converting noncarbohydrate macromolecule
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precursors to glucose or glycogen
21. Ans. (b) Lactate •• Major substrates: Glucogenic amino acids and lactate,
glycerol, and propionate
[Ref. Harper, 26/e p136] •• Major gluconeogenic tissues: Liver (60-90%) and kidney
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accumulation of 2, 3 BPG •• Provides a source of ribose-5-phosphate for nucleic acid
•• One molecule of BPG is bound per Hb tetramer in the biosynthesis
central cavity
•• Role of 2,3 BPG, which is present in high concentration
in tissues, combines with Hb and causes a decrease in the
,3 •• Erythrocytes depends on PPP for NADPH which is required
to maintain glutathione in reduced state which is essential
to maintain integrity of RBC membrane
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affinity for oxygen thus helping oxyhaemoglobin to unload
oxygen and displacing O2 dissociation curve to the right 36. Ans. (d) ATP neither utilized nor produced
•• BPG binds more weakly to fetal Hb than to adult Hb
[Ref. Harper, 26/e p163]
•• Thus, BPG has a less profound effect on HbF & is responsible
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for HbF appearing to have a higher affinity for O2 than does •• Oxidation is achieved by dehydrogenation in PPP/ HMP
HbA pathway (Photograph) the same as in Glycolysis
•• NADP+ is the hydrogen acceptor not NAD+
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