High-Resolution Double-Quantum Deuterium Magic Angle Spinning Solid-State NMR Spectroscopy of Perdeuterated Proteins

被引:25
作者
Agarwal, Vipin [1 ]
Faelber, Katja [1 ]
Schmieder, Peter [1 ]
Reif, Bernd [1 ,2 ]
机构
[1] Leibniz Inst Mol Pharmakol FMP, D-13125 Berlin, Germany
[2] Charite Univ Med Berlin, D-10115 Berlin, Germany
关键词
BETA-AMYLOID FIBRILS; CHEMICAL-SHIFTS; DYNAMICS; H-2; PEPTIDES; RELAXATION; SEPARATION; SPECTRA; C-13;
D O I
10.1021/ja803620r
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
We show in this manuscript that H-2,C-13 correlation spectra in uniformly H-2,C-13 isotopically enriched peptides and proteins can be recorded in MAS solid-state NMR with site specific resolution. A resolved deuterium dimension is obtained by evolving H-2 double-quantum coherences. Experimental H-2 line widths are obtained that are as small as 16 Hz (0.17 ppm at 600 MHz) in the double-quantum dimension. The unprecedented resolution in the deuterium dimension obtained for proteins opens new perspectives for correlation experiments and, in particular, for the characterization of dynamics of proteins in the. solid-state.
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页码:2 / +
页数:4
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