Insights on the conformational stability of collagen

被引：200

作者：

Jenkins, CL

Raines, RT

机构：

[1] Univ Wisconsin, Dept Chem, Madison, WI 53706 USA

[2] Univ Wisconsin, Dept Biochem, Madison, WI 53705 USA

来源：

NATURAL PRODUCT REPORTS | 2002年 / 19卷 / 01期

关键词：

D O I：

10.1039/a903001h

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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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页码：49 / 59

页数：11

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