Multiple Choice
Characterisation of the complete three-dimensional structure of a newly purified protein suggests that it catalyses the breakdown of a large substrate. The protein consists of a single polypeptide chain. It has a large pocket that appears to be the binding site for the substrate and a smaller indentation that appears to be the binding site for a regulatory molecule. What do these structural observations suggest about the mechanism by which the activity of this protein is likely regulated?
A) It is probably an enzyme that is regulated by noncompetitive inhibition.
B) It is probably a multi-subunit enzyme that is regulated by allosteric regulation.
C) It is probably an enzyme that is regulated by competitive inhibition.
D) It is probably an enzyme that is regulated by cooperativity.
Correct Answer:

Verified
Correct Answer:
Verified
Q12: Which of the following statements is true
Q26: Which of the following metabolic processes can
Q27: Which of the following is a primary
Q34: <img src="https://d2lvgg3v3hfg70.cloudfront.net/TB6149/.jpg" alt=" - Activity of
Q36: A decrease in entropy is associated with
Q49: Most cells cannot harness heat to perform
Q55: Which of the following molecules is most
Q55: Which of the following statements describes a
Q58: If an enzyme in solution is saturated
Q67: Which of the following statements describes a