When a polypeptide is in its native conformation, there are weak interactions between its R groups. However, when it is denatured there are similar interactions between the protein groups and water. What then accounts for the greater stability of the native conformation?

In the unfolded polypeptide, there are ordered solvation shells of water around the protein

groups. The number of water molecules involved in such ordered shells is reduced when the protein

folds, resulting in higher entropy. Hence, the lower free energy of the native conformation.

Explanation:

c is the answer because when something is left after something evaporates that shows the chemical change.

because u need two or more forms of the same element that contain equal numbers of protons but different numbers of neutrons in their nuclei to form isotopes.

so since they all have the same shape? i mean maybe because m& m and reeses are both chocolates