Experiments on denaturation and renaturation after the reduction and reoxidation of the -S-S- bonds in the enzyme ribonuclease (RNase) have shown that:
A) folding of denatured RNase into the native, active conformation, requires the input of energy in the form of heat.
B) native ribonuclease does not have a unique secondary and tertiary structure.
C) the completely unfolded enzyme, with all -S-S- bonds broken, is still enzymatically active.
D) the enzyme, dissolved in water, is thermodynamically stable relative to the mixture of amino acids whose residues are contained in RNase.
E) the primary sequence of RNase is sufficient to determine its specific secondary and tertiary structure.

Question

Quizplus · Accepted Answer

The primary sequence of RNase contains all the information necessary for the protein to fold into its specific secondary and tertiary structures, as demonstrated by the ability of denatured RNase to refold into its native, active conformation without additional energy input.

Experiments on Denaturation and Renaturation After the Reduction and Reoxidation