Dynamics and mechanisms of coupled protein folding and binding reactions

被引:110
|
作者
Kiefhaber, Thomas [1 ]
Bachmann, Annett [1 ]
Jensen, Kristine Steen [1 ]
机构
[1] Tech Univ Munich, Dept Chem, Munich Ctr Integrated Prot Sci, D-85747 Garching, Germany
关键词
DISPERSION NMR-SPECTROSCOPY; INTRINSICALLY DISORDERED PROTEINS; TRANSITION-STATE; CONFORMATIONAL SELECTION; CHYMOTRYPSIN INHIBITOR-2; DOMAIN; ASSOCIATION; FRAGMENTS; KINETICS; INTERMEDIATE;
D O I
10.1016/j.sbi.2011.09.010
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
Protein folding coupled to binding of a specific ligand is frequently observed in biological processes. In recent years numerous studies have addressed the structural properties of the unfolded proteins in the absence of their ligands. Surprisingly few time-resolved investigations on coupled folding and binding reactions have been published up to date and the dynamics and kinetic mechanisms of these processes are still only poorly understood. Especially, it is still unsolved for most systems which conformation of the protein is recognized by the ligand (conformational selection vs. folding-after-binding) and whether the ligand influences the folding kinetics. Here we review experimental methods, kinetic models and time-resolved experimental studies of coupled folding and binding reactions.
引用
收藏
页码:21 / 29
页数:9
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