Structural and dynamic studies of proteins by high-resolution solid-state NMR

被引:20
作者
Böckmann, A [1 ]
机构
[1] Univ Lyon 1, CNRS, UMR 5086, IBCP,IFR 128, F-69367 Lyon 7, France
关键词
magic-angle spinning; microcrystalline; protein; solid-state NMR; water-protein interactions;
D O I
10.1016/j.crci.2005.06.008
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Solid-state NMR (SSNMR) spectroscopy provides unique possibilities for the structural investigation of insoluble or non-crystalline molecules (e.g., membrane proteins) at the atomic level. Recent efforts aim at solving the complete structures of biological macromolecules using high-resolution magic-angle spinning NMR. Structurally homogenous samples of [C-13, N-15]-labeled proteins are used in this type of studies. Sequential correlation of resonances, detection of tertiary inter-atomic contacts and characterization of torsion angles can be achieved using multidimensional homo- and heteronuclear correlation experiments. This review discusses the recent progress made in resonances assignments, structure and dynamics determination, as well as the detection of protein interaction partners by SSNMR methods.
引用
收藏
页码:381 / 392
页数:12
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