A heteronuclear direct-detection NMR spectroscopy experiment for protein-backbone assignment

被引：52
|
作者：
Bertini, I
Duma, L
Felli, IC
Fey, M
Luchinat, C
Pierattelli, R
Vasos, PR
机构：
[1] Univ Florence, Magnet Resonance Ctr, I-50019 Florence, Italy
[2] Univ Florence, Dept Chem, I-50019 Florence, Italy
[3] Ecole Normale Super Lyon, Chim Lab, F-69364 Lyon, France
[4] Bruker BioSpin AG, Fallanden, Switzerland
[5] Univ Florence, Dept Agr Biotechnol, I-50019 Florence, Italy
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2004年 / 43卷 / 17期
关键词：
NMR spectroscopy; protein structures; proteins; structure elucidation;
D O I：
10.1002/anie.200453661
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
The starting point of any standard protocol for protein-structure determination by NMR spectroscopy is the sequence-specific resonance assignment of the polypeptide chain. An experiment for determining backbone assignment starts and ends on 13C nuclei and exploits only heteronuclei. This experiment paves a new route for those cases in which the 1H lines are too severely broadened.
引用
收藏
页码：2257 / 2259
页数：3
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