πŸ“Š Biochemistry in Biotechnology
Q. 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
πŸ’¬ Discuss
βœ… Correct Answer: (A) -17.19 kJ mol-1
πŸ“Š Biochemistry in Biotechnology
Q. Oxidation reduction reactions with positive standard redox potential (ΔE°) have
  • (A) Positive ΔG°
  • (B) Negative ΔG°
  • (C) Positive ΔE+
  • (D) Negative ΔE+
πŸ’¬ Discuss
βœ… Correct Answer: (B) Negative ΔG°
πŸ“Š Biochemistry in Biotechnology
Q. 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
πŸ’¬ Discuss
βœ… Correct Answer: (D) Non-competitive inhibition
πŸ“Š Biochemistry in Biotechnology
Q. Which one of the following amino acid residues will destabilize an α-helix when inserted in the middle of the helix?
  • (A) Pro
  • (B) Val
  • (C) Ile
  • (D) Leu
πŸ’¬ Discuss
βœ… Correct Answer: (A) Pro
πŸ“Š Biochemistry in Biotechnology
Q. 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
πŸ’¬ Discuss
βœ… Correct Answer: (C) The velocity of E1 catalyzed reaction is always greater than that of E2
πŸ“Š Biochemistry in Biotechnology
Q. 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
πŸ’¬ Discuss
βœ… Correct Answer: (C) At the carboxy side of the strands
πŸ“Š Biochemistry in Biotechnology
Q. 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
πŸ’¬ Discuss
βœ… Correct Answer: (C) Enzymes do not accelerate the rate of reverse reaction
πŸ“Š Biochemistry in Biotechnology
Q. 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
πŸ’¬ Discuss
βœ… Correct Answer: (C) Valine

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