期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 133, 期 13, 页码 4722-4725出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja200066s
关键词
-
资金
- Max Planck Society
- DFG
- Fondation Bettencourt Schueller
- EMBO
- China Scholarship Council
A strategy for simplified and complete resonance assignment of insoluble and noncrystalline proteins by solid-state NMR (ssNMR) spectroscopy is presented. Proteins produced with [1-C-13]- or [2-C-13]glucose are very sparsely labeled, and the resulting 2D ssNMR spectra exhibit smaller line widths (by a factor of similar to 2 relative to uniformly labeled proteins) and contain a reduced number of cross-peaks. This allows for an accelerated and straightforward resonance assignment without the necessity of time-consuming 3D spectroscopy or sophisticated pulse sequences. The strategy aims at complete backbone and side-chain resonance assignments based on bidirectional sequential walks. The approach was successfully demonstrated with the de novo assignment of the Type Three Secretion System PrgI needle protein. Using a limited set of simple 2D experiments, we report a 97% complete resonance assignment of the backbone and side-chain C-13 atoms.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据