Steady-state fluorescence quenching applications for studying protein structure and dynamics

被引:154
作者
Matyus, Laszlo
Szollosi, Janos
Jenei, Attila
机构
[1] Univ Debrecen, Med & Hlth Sci Ctr, Res Ctr Mol Med, Dept Biophys & Cell Biol, H-4012 Debrecen, Hungary
[2] Univ Debrecen, Hungarian Acad Sci, Cell Biophys Res Grp, H-4012 Debrecen, Hungary
基金
匈牙利科学研究基金会;
关键词
fluorescence quenching; protein structure; FRET; tryptophan fluorescence;
D O I
10.1016/j.jphotobiol.2005.12.017
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
Fluorescence quenching methods are useful to obtain information about the conformational and/or dynamic changes of proteins in complex macromolecular systems. In this review steady-state methods are described and the data interpretation is thoroughly discussed. As a special case of fluorescence quenching mechanism, fluorescence resonance energy transfer (FRET) phenomenon is also presented. Application of a FRET based method to characterize the temperature dependence of the flexibility of protein matrix is clearly demonstrated. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:223 / 236
页数:14
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