期刊
JOURNAL OF MAGNETIC RESONANCE
卷 204, 期 1, 页码 155-159出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jmr.2010.02.003
关键词
Solid-state NMR spectroscopy; Magic-angle spinning; Membrane proteins; Isotope labeling; Structural biology
资金
- Ministere de l'Enseignement Superieur et de la Recherche
- CNRS [UMR 7099, UPR 2301, UMR 8619]
- ANR [ANR-06-JCJC0014]
- Universite Paris Diderot
- Universite Paris-Sud
High-resolution structures of membrane proteins have so far been obtained mostly by X-ray crystallography, on samples where the protein is surrounded by detergent. Recent developments of solid-state NMR have opened the way to a new approach for the study of integral membrane proteins inside a membrane. At the same time, the extension of cell-free expression to the production of membrane proteins allows for the production of proteins tailor made for NMR. We present here an in situ solid-state NMR study of a membrane protein selectively labeled through the use of cell-free expression. The sample consists of MscL (mechano-sensitive channel of large conductance), a 75 kDa pentameric a-helical ion channel from Escherichia coli, reconstituted in a hydrated lipid bilayer. Compared to a uniformly labeled protein sample, the spectral crowding is greatly reduced in the cell-free expressed protein sample. This approach may be a decisive step required for spectral assignment and structure determination of membrane proteins by solid-state NMR. (C) 2010 Elsevier Inc. All rights reserved.
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