Question

Which statement regarding protein structure is true? Van der Waals interactions are insignificant. Hydrophilic side chains are never found in the interior. Hydrophobic side chains are usually in the interior of the native structure. Entropy is generally not a consideration when determining stability.

Answer 1

Answer:

The true statement is Hydrophobic side chains are usually in the interior of the native structure.

Explanation:

In the native structure of a protein, the hydrophobic side chains of aminoacids- such as leucine (Leu), alanine (Ala), methionine (Met), and others-are located in the interior of the structure. They are buried inside the structure, whereas polar side chains are exposed to the outside in the structure, and they interact with water molecules.

Regarding the other statements, entropy-as a measure of disorder of a system-is very important in protein stability as we know that native conformations are more ordered systems, with lower entropy and higher stability. Aminoacids in the protein structure interact each other through Van der Waals interactions and hydrogen bonds.