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

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dc.citation.issue2
dc.citation.volume37
dc.contributor.authorCollier TA
dc.contributor.authorNash A
dc.contributor.authorBirch HL
dc.contributor.authorde Leeuw NH
dc.coverage.spatialEngland
dc.date.available2019-02
dc.date.issued2018-01-30
dc.description.abstractType 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.
dc.description.publication-statusPublished
dc.format.extent537 - 549
dc.identifierhttps://www.ncbi.nlm.nih.gov/pubmed/29380684
dc.identifier.citationJ Biomol Struct Dyn, 2019, 37 (2), pp. 537 - 549
dc.identifier.doi10.1080/07391102.2018.1433553
dc.identifier.eissn1538-0254
dc.identifier.elements-id399147
dc.identifier.harvestedMassey_Dark
dc.languageeng
dc.publisherTaylor & Francis
dc.relation.isPartOfJ Biomol Struct Dyn
dc.relation.urihttps://www.tandfonline.com/doi/abs/10.1080/07391102.2018.1433553
dc.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.
dc.subjectcollagen
dc.subjectcomputational biology
dc.subjectextracellular matrix protein
dc.subjectfibril
dc.subjecthomology modelling
dc.subjectmolecular dynamics
dc.subjectorientation
dc.subjectprotein structure
dc.subjectAmyloid
dc.subjectCollagen
dc.subjectCollagen Type I
dc.subjectHumans
dc.subjectMolecular Dynamics Simulation
dc.subjectStructure-Activity Relationship
dc.subject.anzsrc0601 Biochemistry and Cell Biology
dc.titleRelative orientation of collagen molecules within a fibril: A homology model for homo sapiens type I collagen.
dc.typeJournal article
pubs.notesNot known
pubs.organisational-group/Massey University
pubs.organisational-group/Massey University/College of Sciences
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