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?

Question

Quizplus · Accepted Answer

The formation of covalent bonds between the cysteine residues in the mutant protein would have stabilized the protein structure, resulting in the preservation of the enzymatic activity even after denaturation and refolding. The nonmutant protein lacked this stabilizing interaction, leading to a slight decrease in enzymatic activity after denaturation and refolding.

You Are Trying to Determine Something About the Structure of a Particular