Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution

被引:261
作者
Igumenova, Tatyana I.
Frederick, Kendra King
Wand, A. Joshua [1 ]
机构
[1] Univ Penn, Johnson Res Fdn, Philadelphia, PA 19104 USA
[2] Univ Penn, Dept Biochem & Biophys, Philadelphia, PA 19104 USA
关键词
D O I
10.1021/cr040422h
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Nuclear magnetic resonance (NMR) spectroscopy is at the core of current efforts to illuminate the nature and protein dynamics and their role in biological function. This review attempts to provide a complete description of the theoretical and technical foundation for solution NMR relaxation methods that are currently being brought to bear on fast sub-nanosecond protein side chain dynamics. A survey of basic observations about the side chain dynamics derived from NMR relaxation studies is presented along with several analyses meant to dispel commonly held but apparently inaccurate correlations between dynamics, structure, and function. How dynamics can enter into fundamental thermodynamic and kinetic aspects of proteion function is illustrated with results from several systems that point to promising future for this area of inquiry.
引用
收藏
页码:1672 / 1699
页数:28
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