
The structure of collagen was worked out by G. N. Ramachandran (famous for his Ramachandran plots). The molecule consists of three left-handed helical chains coiled around each other to form a right-handed supercoil. Each lefthanded helix in collagen has 3.0 amino acid residues per turn and a pitch of 0.94 nm, giving a rise of 0.31 nm per residue.

In addition to hydroxyproline, collagen contains an additional modified amino acid residue called 5-hydroxylysine. Some hydroxylysine residues are covalently bonded to carbohydrate residues, making collagen a glycoprotein. The role of this glycosylation is not known.

Collagen triple helices aggregate in a staggered fashion to form strong, insoluble fibers. The strength and rigidity of collagen fibers result in part from covalent cross-links. The groups of the side chains of some lysine and hydroxylysine residues are converted enzymatically to aldehyde groups producing allysine and hydroxyallysine residues. Allysine residues (and their hydroxy derivatives) react with the side chains of lysine and hydroxylysine residues to form Schiff bases, complexes formed between carbonyl groups and amines. These Schiff bases usually form between collagen molecules.


(Collagen molecular image originally produced by J.W. Schmidt for Wikepedia. GNU Free Documentation License)
(Text from Horton et al. Principles of Biochemistry 4th ed.© Pearson Prentice Hall, Inc.)