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

页码：2257 / 2259

页数：3

共 14 条

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