30. The immediate electron donor to P680+ is a
(A) leucine,
(B) tryptophan,
(C) serine,
(D) histidine,
(E) tyrosine residue.

31. Nucleotides have a nitrogenous base linked to a sugar by a: (A) α-anhydride bond, (B) β-ester bond, (C) α-N-amide bond, (D) B-N-acetal (glycosidic) bond, (E) α-N-hemiacetal bond.

32. The pitch, or distance required to complete one helical turn in B-DNA is (A) 33.2 Å, (B) 45.6 Å, (C) 38.4 Å, (D) 24.6 Å, (E) 28.4 Å.

33. What is this molecule below (and its conformation)? (A) anti A, (B) syn U, (C) anti T, (D) anti G, (E) syn C. 

34. The function of DNA topoisomerases is: (A) packaging DNA into nucleosomes, (B) forming cruciform DNA, (C) unwinding G:C rich areas in DNA, (D) breaking one or more strands of DNA, winding them tighter or looser, and rejoining the ends, (E) promoting DNA hybridization.

35. Successive base pairs in B-DNA show a rotation with respect to each other (so-called helical twist) of (A) 34°, (B) 36°, (C) 38°, (D) 32°, (E) 40°.

36. If the rate constant for the enzyme catalyzed reaction is 1 x 105/sec and the rate constant for the uncatalyzed reaction is 2 x 10/sec, the catalytic power of the enzyme is: (A) 2, (B) (C) (D) 5 x 109, (E)

37. All of the following statements are true about the relationships between [S], and EXCEPT: (A) As [S] is increased, v approaches the limiting value, , (B) = /2, (C) The rate of the reaction, v, follows a first order rate equation v = K'[A] and K' = (D) The rate of product formed, v, is at when [S] ＞＞ , (E) assist in finding the rate of the enzyme catalyzed reaction only if the reaction is irreversible.

38. In uncompetitive inhibition: (A) I combines only with ES, (B) I combines only with E, (C) I combines with E and ES, (D) I combines with EP, (E) none of the above.

39. Formation of the ES complex results in (A) entropy gain, (B) enthalpy gain, (C) entropy loss, (D) enthalpy loss, (E) none of the above.

40. Which statement is correct about the Michaelis-Menten constant, , for the kinetic mechanism below?(A) It is numerically equal to the substrate concentration required to achieve one half the maximum velocity, (B) It's defined as ,(C) It is approximately equal to the dissociation constant for the enzyme-substrate complex to E + P, (D) The value of is constant for an enzyme regardless of the specific substrate molecule used to determine it, (E) Its numeric value has the units of . 

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