The in situ supermolecular structure of type I collagen

Orgel, Joseph P. R. O., Miller, Andrew, Irving, Thomas C., Fischetti, Robert F., Hammersley, Andrew P. and Wess, Timothy James 2001. The in situ supermolecular structure of type I collagen. Structure 9 (11) , pp. 1061-1069. 10.1016/S0969-2126(01)00669-4

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Abstract

Background: The proteins belonging to the collagen family are ubiquitous throughout the animal kingdom. The most abundant collagen, type I, readily forms fibrils that convey the principal mechanical support and structural organization in the extracellular matrix of connective tissues such as bone, skin, tendon, and vasculature. An understanding of the molecular arrangement of collagen in fibrils is essential since it relates molecular interactions to the mechanical strength of fibrous tissues and may reveal the underlying molecular pathology of numerous connective tissue diseases. Results: Using synchrotron radiation, we have conducted a study of the native fibril structure at anisotropic resolution (5.4

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Optometry and Vision Sciences
Subjects:	Q Science > QR Microbiology
Uncontrolled Keywords:	collagen; extracellular matrix; structure; X-ray diffraction; packing; fibril
ISSN:	1545-9985
Last Modified:	19 Mar 2016 22:02
URI:	https://orca.cardiff.ac.uk/id/eprint/809

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