Design of β-sheet systems for understanding the thermodynamics and kinetics of protein folding

被引：95

作者：

Searle, MS

Ciani, B

机构：

[1] Ctr Biomol Sci, Sch Chem, Nottingham NG7 2RD, England

[2] Univ Manchester, Sch Biol Sci, Manchester M13 9PT, Lancs, England

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2004年 / 14卷 / 04期

关键词：

D O I：

10.1016/j.sbi.2004.06.001

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：

Peptide beta-sheet systems have emerged as context-independent models for probing secondary structure propensities, the nature and magnitude of stabilizing weak interactions, and aspects of cooperativity both parallel and perpendicular to the strand direction. These systems have allowed fundamental advances in understanding non-covalent interactions relevant to both chemical and biological systems, and in describing the protein folding energy landscape.

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收藏

页码：458 / 464

页数：7

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