Stabilization of the collagen structure by hydroxyproline residues
- Cite this article as:
- Bansal, M., Ramakrishnan, C. & Ramachandran, G.N. Proc. Indian Acad. Sci. (1975) 82: 152. doi:10.1007/BF03046724
- 57 Downloads
The molecular structure of collagen is now accepted to be based on a triple-stranded coiled-coil, in which the three strands are held together predominantly by hydrogen bonds. Recent experimental evidence has shown that the presence of hydroxyproline residues in the third position of the repeating tripeptide unit lends additional stability to the collagen structure. In this paper, we report a model structure, which is supported by these observations. In a model structure proposed earlier, there are two hydrogen bonds per tripeptide unit, one of which is a direct interchain hydrogen bond, while the second hydrogen bond can be formedvia a water molecule. It has now been shown that the same water molecule can also form a hydrogen bond with the oxygen of theγ-hydroxyl group of hydroxyproline in the third position in the sequence (Gly-R2-R3).
This hydroxyl group can also take part in an inter-triple-helix hydrogen bond. Our studies thus show the role played by hydroxyproline residues in the structure and stability of collagen.