Fourier transform of the collagen triple-helical structure and its significance

Bansal, M (1977) Fourier transform of the collagen triple-helical structure and its significance. In: Pramana, 9 (4). pp. 339-347.

PDF fulltextv.pdf - Published Version Restricted to Registered users only Download (494kB) | Request a copy

Abstract

The Fourier transforms of the collagen molecular structure have been calculated taking into consideration various side chain atoms, as well as the presence of bound water molecules. There is no significant change in the calculated intensity distribution on including the side chain atoms of non-imino-acid residues. Taking into account the presence of about two bound water molecules per tripeptide unit, the agreement with the observed x-ray pattern is slightly improved. Fourier transforms have also been calculated for the detailed molecular geometries proposed from other laboratories. It is found that there are no major differences between them, as compared to our structure, either in the positions of peak intensity or in the intensity distribution. Hence it is not possible to judge the relative merits of the various molecular geometries for the collagen triple helix from a comparison of the calculated transforms with the meagre data available from its x-ray fibre pattern. It is also concluded that the collagen molecular structure should be regarded as a somewhat flexible chain structure, capable of adapting itself to the requirements of the different side groups which occur in each local region.

Item Type:	Journal Article
Publication:	Pramana
Publisher:	Sprigner Link
Additional Information:	Copyright of this article belongs to Sprigner Link.
Keywords:	Collagen molecular structure; Fourier transforms; water-bound collagen triple helix
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	06 Feb 2010 05:40
Last Modified:	19 Sep 2010 05:49
URI:	http://eprints.iisc.ac.in/id/eprint/24196

Actions (login required)

View Item