**Core Concept:**
The question is about the alpha helix structure in proteins, which is a right-handed helical secondary structure found in many proteins. The alpha helix is stabilized by hydrogen bonds between the backbone amide nitrogen and carbonyl oxygen atoms of adjacent residues. These hydrogen bonds occur at regular intervals, which leads to the characteristic bend in the helix.

**Why the Correct Answer is Right:**
Glycine is the amino acid that contributes to the formation of the bends in the alpha helix structure. Its small size allows it to fit into the narrow helical groove and its amide group is hydrogen bonded to the carbonyl group of the next residue, resulting in the regular bends in the alpha helix.

**Why Each Wrong Option is Incorrect:**
A) Alanine: Alanine has a larger side chain than glycine, which would not allow it to fit into the narrow helical groove, thus making it unsuitable for forming bends in the alpha helix.
B) Arginine: Arginine has a large guanidinium group that would not fit into the narrow helical groove, making it an unsuitable amino acid for forming bends in the alpha helix.
C) Proline: Proline has a bulky imidazole group, which would not allow it to fit into the narrow helical groove, thus making it unsuitable for forming bends in the alpha helix.
D) Serine: Serine has a small side chain, but it lacks the hydroxyl group that is required for hydrogen bonding, which is essential for forming bends in the alpha helix.

**Clinical Pearl:**
Understanding the role of amino acids in the alpha helix structure is crucial for medical students, as it has implications in protein folding, stability, and function. The regular bends in the alpha helix are essential for maintaining the helix's stability and allowing proteins to fold into their specific three-dimensional structures, which are essential for their biological activity.