The Most Important Contribution to the Stability of a Protein's

Multiple Choice

The most important contribution to the stability of a protein's conformation appears to be the:

A) entropy increase from the decrease in ordered water molecules forming a solvent shell around it.
B) maximum entropy increase from ionic interactions between the ionized amino acids in a protein.
C) sum of free energies of formation of many weak interactions among the hundreds of amino acids in a protein.
D) sum of free energies of formation of many weak interactions between its polar amino acids and surrounding water.
E) stabilizing effect of hydrogen bonding between the carbonyl group of one peptide bond and the amino group of another.