Match items in
Group I with
Group II .
Group I
Group II
P. Glycolytic pathway
1. Chloroplast
Q. Eukaryotic oxidative metabolism
2. Glyoxysomes
R. Glyoxylate cycle
3. Mitochondria
S. Calvin cycle
4. Cytosol
A. P-1, Q-2, R-3, S-4
B. P-2, Q-3, R-4, S-1
C. P-4, Q-3, R-2, S-1
D. P-3, Q-4, R-1, S-2
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The value of ΔG°, if given Kep is 1.7, at 23°C will be
A. -17.19 kJ mol-1
B. -19.8 kJ mol-1
C. +52.82 kJ mol-1
D. -117.07 kJ mol-1
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Oxidation reduction reactions with positive standard redox potential (ΔE°) have
A. Positive ΔG°
B. Negative ΔG°
C. Positive ΔE+
D. Negative ΔE+
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Identify the enzyme that catalyzes the following reaction.
α - Ketoglutarate + N A D H + N H 4 + + H + → Glutamate + N A D + + H 2 O
A. Glutamate synthetase
B. Glutamate oxoglutarate aminotransferase
C. Glutamate dehydrogenase
D. α-Ketoglutarate deaminase
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Match the following photoreceptors with their prosthetic groups and spectral specificity
Photoreceptor
Moiety that absorbs light
Absorption (nm)
P. Phototropin
1. Chromobilin
a. 400 - 500
Q. Cryptochrome
2. FAD
b. 600 - 800
R. Phytochrome
3. FMN
c. 500 - 600
A. P-3-a, Q-2-a, R-1-b
B. P-1-b, Q-1-a, R-3-b
C. P-3-a, Q-1-a, R-1-c
D. P-2-c, Q-1-c, R-1-a
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The degree of inhibition for an enzyme catalyzed reaction at a particular inhibitor concentration is independent of initial substrate concentration. The inhibition follows
A. Competitive inhibition
B. Mixed inhibition
C. Uncompetitive inhibition
D. Non-competitive inhibition
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Which one of the following amino acid residues will destabilize an α-helix when inserted in the middle of the helix?
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Determine the correctness or otherwise of the following Assertion (A) and Reason (R) .
Assertion: Plants convert fatty acids into glucose.
Reason: Plants have peroxisomes.
A. Both (A) and (R) are true but (R) is not the correct reason for (A)
B. Both (A) and (R) are true and (R) is the correct reason for (A)
C. (A) is true but (R) is false
D. (A) is false but (R) is true
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The turnover numbers for the enzymes E1 and E2 are 150 s-1 and 15 s-1 respectively. This means
A. E1 binds to its substrate with higher affinity than E2
B. The velocity of reactions catalyzed by E1 and E2 at their respective saturating substrate concentrations could be equal, if concentration of E2 used is 10 times that of E1
C. The velocity of E1 catalyzed reaction is always greater than that of E2
D. The velocity of E1 catalyzed reaction at a particular enzyme concentration and saturating substrate concentration is lower than that of E2 catalyzed reaction under the same conditions
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Match the chemicals in
Group I with the possible type/class in
Group II .
Group I
Group II
P. Picloram
1. Vitamin
Q. Zeatin
2. Auxin
R. Thiamine
3. Amino Acid
S. Glutamine
4. Cytokinin
A. P-2, Q-4, R-1, S-3
B. P-4, Q-1, R-2, S-3
C. P-3, Q-1, R-2, S-4
D. P-4, Q-2, R-1, S-3
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A protein without its prosthetic group is known as
A. Apoprotein
B. Hemoprotein
C. Holoprotein
D. lipoprotein
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The active site in the alpha/beta barrel structures is usually located
A. Inside the barrel
B. At the amino side of the strands
C. At the carboxy side of the strands
D. At any arbitrary site
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Identify the statement that is not applicable to an enzyme catalyzed reaction.
A. Enzyme catalysis involves propinquity effects
B. The binding of substrate to the active site causes a strain in the substrate
C. Enzymes do not accelerate the rate of reverse reaction
D. Enzyme catalysis involves acid-base chemistry
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Amino acid residue which is most likely to be found in the interior of water-soluble globular proteins is
A. Threonine
B. Aspartic acid
C. Valine
D. Histidine
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In N-linked glycosylation, the oligosaccharide chain is attached to protein by
A. Asparagine
B. Arginine
C. Serine
D. Threonine
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Which of the following components constitute a molecular mechanics force field?
P. Bond stretching
Q. Bond angle bending
R. Torsional bond rotation
S. Non-bonded interactions
A. P and Q only
B. P, Q and R only
C. P, Q and S only
D. P, Q, R and S
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Which one of the following is an ABC transporter?
A. Multidrug resistance protein
B. Acetylcholine receptor
C. Bacteriorhodopsin
D. ATP synthase
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Natural proteins are composed primarily of 20 α-amino acids. Which one of the following statements is true for any of these amino acids in a solution of pH 1.5?
A. Only the amino group is ionized
B. Only the carboxylic acid group is ionized
C. Both amino and carboxylic acid groups are ionized
D. Both amino and carboxylic add groups are neutral
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Which one of the following statements is NOT true?
A. In competitive inhibition, substrate and inhibitor compete for the same active site of an enzyme
B. Addition of a large amount of substrate to an enzyme cannot overcome uncompetitive inhibition
C. A transition state analogue in enzyme catalyzed reaction increases the rate of product formation
D. In non-competitive inhibition, KM of an enzyme for its substrate remains constant as the concentration of the inhibitor increases
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Analysis of a hexapeptide using enzymatic cleavage reveals the following result:
• Amino acid composition of the peptide is: 2R, A, V, S, Y
• Trypsin digestion yields two fragments and the compositions are: (R, A, V) and (R, S, Y)
• Chymotrypsin digestion yields two fragments and the compositions are: (A, R, V, Y) and (R, S)
• Digestion with carboxypeptidase A yields no cleavage product.
Given: Trypsin cleaves at carboxyl side of R. Chymotrypsin cleaves at carboxyl side of Y. Carboxypeptidase A cleaves at amino side of the C-terminal amino acid (except R and K) of the peptide.
The correct amino acid sequence of the peptide is:
A. RSYRVA
B. AVRYSR
C. SRYVAR
D. SVRRYA
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