A peptide bond
A) contributes atoms to hydrophobic interactions.
B) exhibits unrestricted rotation around the C-N bond.
C) is formed between the side chains of Glu and Lys residues.
D) is planar and partially ionic.

Question

Quizplus · Accepted Answer

A peptide bond is a covalent bond formed between the carboxyl group (C=O) of one amino acid and the amino group (NH3+) of another amino acid. This bond is planar and partially ionic due to the resonance structures that can be formed. The double-bond character of the C-N bond results in restricted rotation, which gives the peptide backbone its characteristic rigidity. Peptide bonds do not contribute atoms to hydrophobic interactions, as they involve polar groups. Additionally, peptide bonds are not formed between the side chains of Glu and Lys residues specifically, as any two amino acids can form a peptide bond.

A Peptide Bond