Relative orientation of collagen molecules within a fibril: a homology model for homo sapiens type I collagen

Collier, Thomas A., Nash, Anthony, Birch, Helen L. and De Leeuw, Nora ORCID: https://orcid.org/0000-0002-8271-0545 2019. Relative orientation of collagen molecules within a fibril: a homology model for homo sapiens type I collagen. Journal of Biomolecular Structure and Dynamics 37 (2) , pp. 537-549. 10.1080/07391102.2018.1433553

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Abstract

Type I collagen is an essential extracellular protein that plays an important structural role in tissues that require high tensile strength. However, owing to the molecule’s size, to date no experimental structural data are available for the Homo sapiens species. Therefore, there is a real need to develop a reliable homology model and a method to study the packing of the collagen molecules within the fibril. Through the use of the homology model and implementation of a novel simulation technique, we have ascertained the orientations of the collagen molecules within a fibril, which is currently below the resolution limit of experimental techniques. The longitudinal orientation of collagen molecules within a fibril has a significant effect on the mechanical and biological properties of the fibril, owing to the different amino acid side chains available at the interface between the molecules.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Chemistry
Publisher:	Taylor & Francis
ISSN:	0739-1102
Date of First Compliant Deposit:	5 March 2018
Date of Acceptance:	23 January 2018
Last Modified:	03 May 2023 22:52
URI:	https://orca.cardiff.ac.uk/id/eprint/109680

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