Tuesday, February 27, 2007


Collagen is the major protein component of the connective tissue of vertebrates; it constitutes about 25% to 35% of the total protein in mammals. Collagen molecules have remarkably diverse forms and functions. For example, collagen in tendons forms stiff, ropelike fibers of tremendous tensile strength; in skin, collagen takes the form of loosely woven fibers, permitting expansion in all directions.

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.

The collagen triple helix is stabilized by interchain hydrogen bonds. The sequence of the protein in the helical region consists of multiple repeats of the form –Gly–X–Y–, where X is often proline and Y is often a modified proline called 4-hydroxyproline. The glycine residues are located along the central axis of the triple helix, where tight packing of the protein strands can accommodate no other residue. For each –Gly–X–Y– triplet, one hydrogen bond forms between the amide hydrogen atom of glycine in one chain and the carbonyl oxygen atom of residue X in an adjacent chain. Hydrogen bonds involving the hydroxyl group of hydroxyproline may also stabilize the collagen triple helix. Unlike the more common α helix, the collagen helix has no intrachain hydrogen bonds.

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.

Hydroxyproline and hydroxylysine residues are formed when specific proline and lysine residues are hydroxylated after incorporation into the polypeptide chains of collagen. The hydroxylation reactions are catalyzed by enzymes and require ascorbic acid (vitamin C).

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 molecules associate to form long thick fibres with a characteristic banded appearance. These thick fibres confer strength and flexibility to many tissues.

(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.)


  1. Laurence...wonderful information. this was very useful in my own biochemistry course.

  2. I found this article very useful and relevant to a paper I had to write for my own biochemistry class. Great work.
    Thanks again.

  3. Can i ask something ? Well, can you get collagen from aquatic animals? i mean, marine collagen ?

  4. Thank you so much for this entry professor. It is just simple enough to explain the biochemical properties of collagen without delving too deep.

  5. Thanks. The article explained interchain bonding much better than my professor.