Fully folded proteins typically have polar side chains on their surfaces, where electrostatic attractions and hydrogen bonds can form between the polar group on the amino acid and the polar molecules in the solvent. In contrast, some proteins have a polar side chain in their hydrophobic interior. Which of the following would not occur to help accommodate an internal, polar side chain?
(a) A hydrogen bond forms between two polar side chains.
(b) A hydrogen bond forms between a polar side chain and the protein backbone.
(c) A hydrogen bond forms between a polar side chain and an aromatic side chain.
(d) Hydrogen bonds form between polar side chains and a buried water molecule.
Answer: C