Question

1st attempt See Hint When a protein folds, transitioning from denatured to native state, the change in free energy is favorable (AG<0). In general, the entropic change is (A) due to the more limited number of conformations. The enthalpic change is (B) due to the many weak interactions that are formed. With the exception of disulfide bonds, weak interactions include the formation of (C) and numerous (D) . in the native state.

Answer 1

The answers of the fill-in blanks are mentioned below along with explanations :

(A) Unfavorable
(B) Favorable
(C) Hydrogen
(D) Van der Waals

During protein folding, entropic changes are unfavorable since the backbone conformations are more restricted, leading to a more ordered system. Enthalpic changes are favorable since many new favorable hydrogen bonds and van der Waals interactions are generally formed