Relative orientation of collagen molecules within a fibril: a homology model for homo sapiens type I collagen |
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Authors: | Thomas A. Collier Anthony Nash Helen L. Birch |
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Affiliation: | 1. Institute of Natural and Mathematical Sciences, Massey University, Auckland 0632, New Zealand;2. Department of Physiology, Anatomy and Genetics, University of Oxford, South Parks Road, Oxford OX1 3QX, UK;3. Institute of Orthopaedics and Musculoskeletal Science, UCL, RNOH Stanmore Campus, London, UK |
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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. |
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Keywords: | collagen molecular dynamics extracellular matrix protein computational biology homology modelling protein structure fibril orientation |
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