The most important repeating unit in the collagen alpha chain is the Gly–X–Y motif, where:
Why glycine?
Because it’s the smallest amino acid, with only a hydrogen atom as its side chain. This minimal steric hindrance allows the three chains to pack tightly together. In the central axis of the triple helix, no other amino acid is small enough to fit without disrupting the structure.
If glycine is replaced by a bulkier residue (as in some mutations), the tight packing is disturbed, leading to improper folding and structurally weak collagen — which is the root cause of osteogenesis imperfecta.
❌ Why the Other Options Are Incorrect:
Confers rigidity to the collagen molecule
→ That function is primarily due to proline and hydroxyproline, which impose conformational constraints. Glycine, being flexible and small, doesn’t contribute rigidity.
Exists in D and L forms
→ Although amino acids can exist in D and L forms, only L-amino acids are used in mammalian proteins. This has no relevance to glycine’s specific role in collagen structure.
Is hydroxylated easily
→ It’s proline and lysine, not glycine, that undergo hydroxylation to form hydroxyproline and hydroxylysine — important for collagen crosslinking and stability, but unrelated to glycine’s positional significance.
Is a polar amino acid
→ Glycine is technically non-polar, although it’s often referred to as ambivalent. Regardless, its polarity is not the reason it appears every third residue in collagen. The key reason is its small size.