Long-Range Correlations between Aliphatic 13C Nuclei in Protein MAS NMR Spectroscopy

被引：33
作者：
Bayro, Marvin J. [1 ,2 ]
Maly, Thorsten [1 ,2 ]
Birkett, Neil R. [3 ]
Dobson, Christopher M. [3 ]
Griffin, Robert G. [1 ,2 ]
机构：
[1] MIT, Francis Bitter Natl Magnet Lab, Cambridge, MA 02139 USA
[2] MIT, Dept Chem, Cambridge, MA 02139 USA
[3] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2009年 / 48卷 / 31期
基金：
美国国家卫生研究院;
关键词：
amyloid fibrils; dipolar recoupling; magic-angle spinning; NMR spectroscopy; protein structures; ANGLE-SPINNING NMR; SOLID-STATE NMR; ROTATING SOLIDS; CROSS-POLARIZATION; DIFFUSION; RESONANCE; EXCHANGE;
D O I：
10.1002/anie.200901520
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Highly efficient polarization transfer can be achieved in the magic-angle spinning NMR analysis of proteins by the combination of 13C labeling at alternating positions and band-selective radio-frequency-driven recoupling (BASE RFDR), a pulse scheme aimed at exploiting the bandwidth selectivity and favorable effects of weak 13C radio-frequency irradiation to reintroduce the homonuclear dipolar interactions between distant nuclei. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码：5708 / 5710
页数：3
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