Complete assignment of heteronuclear protein resonances by protonless NMR spectroscopy

被引：148

作者：

Bermel, W

Bertini, I

Duma, L

Felli, IC

Emsley, L

Pierattelli, R

Vasos, PR

机构：

[1] Univ Florence, CERM, I-50019 Sesto Fiorentino, Italy

[2] Univ Florence, Dept Chem, I-50019 Sesto Fiorentino, Italy

[3] Bruker BioSpin GmbH, Rheinstetten, Germany

[4] Ecole Normale Super Lyon, CNRS, UMR 5182, Chim Lab, F-69364 Lyon, France

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2005年 / 44卷 / 20期

关键词：

carbon NMR spectroscopy; NMR spectroscopy; protein structures; proteins; spin-state selection;

D O I：

10.1002/anie.200461794

中图分类号：

O6 [化学];

学科分类号：

0703 [化学];

摘要：

(Chemical Equation Presented) The detection of 13C is now amenable to high-resolution NMR spectroscopy of proteins. A protocol for 13C homonuclear decoupling in multidimensional experiments correlates carbonyl, Cα, and Cβ nuclei (see picture). These techniques also allow the detection of side-chain nuclei in exclusively heteronuclear experiments, and thus the complete assignment of proteins. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA.

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页码：3089 / 3092

页数：4

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