Measuring protein conformational changes by FRET/LRET

被引：170

作者：

Heyduk, T ^{[1
]}

机构：

[1] St Louis Univ, Sch Med, EA Doisy Dept Biochem & Mol Biol, St Louis, MO 63104 USA

来源：

CURRENT OPINION IN BIOTECHNOLOGY | 2002年 / 13卷 / 04期

关键词：

D O I：

10.1016/S0958-1669(02)00332-4

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Fluorescence resonance energy transfer (FRET) provides a unique means of measuring interatomic distances in biological molecules in real time. Recent advances have been made in the application of this technique to studies of conformational changes in proteins. New ways of introducing fluorescence probes into proteins, newly developed fluorescence probes, and progress in the technologies for fluorescence signal detection have greatly expanded the range of applications of FRET. In particular, studies of conformational changes in proteins at a single molecule level and in the native in vivo context of a living cell are now possible.

引用

页码：292 / 296

页数：5

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