A hypothesis on the role of hydroxyproline in stabilizing collagen structure

Ramachandran, GN and Bansal, M and Bhatnagar, RS (1973) A hypothesis on the role of hydroxyproline in stabilizing collagen structure. In: Biochimica et Biophysica Acta (BBA) - Protein Structure, 322 (1). pp. 166-171.

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Abstract

The possibility of hydroxyproline residues stabilizing the collagen triple-helical structure by the formation of additional hydrogen bonds through their γ-hydroxyl group has been studied from structural considerations. It is not possible for this hydroxyl group to form a direct hydrogen bond with a suitable group in a neighbouring chain of the triple-helical protofibril. However, in the modified one-bonded structure, which is stabilized by additional hydrogen bonds being formed through water molecules as intermediaries (put forward in 1968 by Ramachandran, G. N. and Chandrasekharan, R.), it is found that the γ-hydroxyl group of hydroxyproline can form a good hydrogen bond with the water oxygen as acceptor, the hydrogen bond length being 2.82 Å. It is proposed that, in addition to stabilizing the collagen triple-helical structure due to the stereochemical properties of the pyrrolidine ring, hydroxyproline gives added stability by the formation of an extra hydrogen bond. Experimental studies on the determination of shrinkage and denaturation temperatures of native collagen and its synthetic analogues, as a function of their hydroxyproline content, are being undertaken to test this hypothesis.

Item Type:	Journal Article
Publication:	Biochimica et Biophysica Acta (BBA) - Protein Structure
Publisher:	Elsevier Science
Additional Information:	Copy right of this article belongs to Elsevier Science.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	08 Jan 2010 05:04
Last Modified:	19 Sep 2010 05:44
URI:	http://eprints.iisc.ac.in/id/eprint/23045

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