Structural analysis of non-native states of proteins by NMR methods

被引：182

作者：

Shortle, DR

机构：

[1] Department of Biological Chemistry, Johns Hopkins Univ. Sch. of Medicine, Baltimore, MD 21205

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1996年 / 6卷 / 01期

关键词：

D O I：

10.1016/S0959-440X(96)80091-1

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：

Established NMR methods are increasingly being applied to the non-native states of proteins. For small denatured proteins, full assignment of proton, N-15 and C-13 resonances is often straightforward. Sensitive methods exist for detecting fractionally populated alpha helices and beta strands, but defining transient interactions among side chains is proving more problematic. The non-native states of several small proteins are being intensively investigated to address a number of questions about protein folding.

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页码：24 / 30

页数：7

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