Type I collagen, the most abundant collagen type found in human connective tissues such as skin, tendons, bones, and ligaments, has a very unique amino acid composition. Among the various amino acids found in collagen, glycine is the most abundant, comprising approximately 30% of the total amino acid content in Type I collagen.
Glycine is crucial for the structure of collagen because it is the smallest amino acid and occupies every third position in the repeating tri-peptide sequence (Gly-X-Y), where X and Y are often proline and hydroxyproline. This repetitive glycine pattern is fundamental for the formation of the collagen triple helix structure, which provides collagen with its strength and stability.
While proline is also highly abundant in collagen, it is glycine that dominates in terms of percentage. Methionine and guanosine, on the other hand, are not significantly present in collagen’s structure.
Type I collagen's amino acid sequence is critical for its role in maintaining the structural integrity of tissues, and glycine plays a key role in enabling the tight coiling of collagen’s triple-helix.