Relative orientation of collagen molecules within a fibril: A homology model for homo sapiens type I collagen.
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Date
2018-01-30
Open Access Location
Authors
Journal Title
Journal ISSN
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Publisher
Taylor & Francis
Rights
© 2018 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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.
Description
Keywords
collagen, computational biology, extracellular matrix protein, fibril, homology modelling, molecular dynamics, orientation, protein structure, Amyloid, Collagen, Collagen Type I, Humans, Molecular Dynamics Simulation, Structure-Activity Relationship
Citation
J Biomol Struct Dyn, 2019, 37 (2), pp. 537 - 549