Time-resolved biophysical methods in the study of protein folding

被引：117

作者：

Plaxco, KW

Dobson, CM

机构：

[1] New Chemistry Laboratory, University of Oxford, Oxford OX1 3QT, South Parks Road

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1996年 / 6卷 / 05期

基金：

英国工程与自然科学研究理事会; 英国医学研究理事会;

关键词：

D O I：

10.1016/S0959-440X(96)80029-7

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：

Many of the biophysical techniques developed to characterize native proteins at equilibrium have now been adapted to the structural and thermodynamic characterization of transient intermediate populations during protein folding. Recent advances in these techniques, the use of novel methods of initiating refolding, and a convergence of theoretical and experimental approaches are leading to a detailed understanding of many aspects of the folding process.

引用

收藏

页码：630 / 636

页数：7

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