Issue 1, 2002
From the journal:

Natural Product Reports

Insights on the conformational stability of collagen

Cara L. Jenkinsa  and  Ronald T. Raines*a  

* Corresponding authors

a Department of Chemistry and Department of Biochemistry, University of Wisconsin–Madison, Madison, USA

Abstract

Covering: 1994 to mid-2001

This review describes work on the conformational stability of the collagen triple helix. In 1994, the structure of collagen was determined at high resolution. Since then, much work has been done on synthetic mimics of collagen that contain host–guest peptides, tethers, peptoid residues, or analogs of the prevalent 4(R)-hydroxy-L-proline residues. This work has revealed much about the chemical basis for collagen stability, and could spawn useful new biomaterials. The literature from 1994 to mid 2001 is reviewed, and 116 references are cited.

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Article information

DOI
https://doi.org/10.1039/A903001H
Article type
Review Article
Submitted
28 Aug 2001
First published
10 Dec 2001

Nat. Prod. Rep., 2002,19, 49-59

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Insights on the conformational stability of collagen

C. L. Jenkins and R. T. Raines, Nat. Prod. Rep., 2002, 19, 49 DOI: 10.1039/A903001H

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