Multiple Choice
You are trying to determine something about the structure of a particular enzyme.For one of your experiments, you mutate the protein to include some cysteine residues in sections you think might be folded close to each other.You place properly folded original proteins and mutant proteins into a denaturing solution (urea) , then back into a physiological solution.You find that the mutant has 100 percent enzymatic activity while the nonmutant protein has 90 percent enzymatic activity.What is the best explanation for this observation?
A) Urea bound to cysteine residues, stabilizing the protein structure.
B) The cysteine residues formed a covalent bond that was not broken during denaturation, thus stabilizing protein structure.
C) The cysteine residues destabilized the structure.
D) Proteins without cysteine residues cannot fold back to their native shape after denaturation.
E) Adding cysteine residues gave the enzyme a more reactive active site.
Correct Answer:
Verified
Correct Answer:
Verified
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