Protein solid-state NMR resonance assignments from (13C, 13C) correlation spectroscopy

被引：48
|
作者：
Seidel, K [1 ]
Lange, A [1 ]
Becker, S [1 ]
Hughes, CE [1 ]
Heise, H [1 ]
Baldus, M [1 ]
机构：
[1] Max Planck Inst Biophys Chem, Dept NMR Based Struct Biol, D-37077 Gottingen, Germany
来源：
PHYSICAL CHEMISTRY CHEMICAL PHYSICS | 2004年 / 6卷 / 22期
关键词：
D O I：
10.1039/b411689e
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
It is demonstrated that sequential resonance assignments can be obtained from (C-13, C-13) correlation spectroscopy on a uniformly labeled protein under magic angle spinning. The experiment relies on weak (C', Calpha) coupling conditions using a defined range of MAS rates and can be employed at arbitrary magnetic. eld strength.
引用
收藏
页码：5090 / 5093
页数：4
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