期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 56, 期 9, 页码 2508-2512出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201610441
关键词
coplymers; membrane proteins; nanodiscs; NMR spectroscopy; solid-state NMR
资金
- European Research Council [ERC-StG 311318-ProtDyn2Function]
- CEA
- CNRS
- Universite Grenoble Alpes
- Seventh Framework Program of the European Union (Marie Curie Initial Training Network ManiFold) [317371]
- FRISBI [ANR-10-INSB-05-02]
- GRAL [ANR-10-LABX-49-01]
- Rhone-Alpes Region
- Fondation Recherche Medicale (FRM)
- fonds FEDER
- GIS-Infrastructures en Biologie Sante et Agronomie (IBISA)
The structure, dynamics, and function of membrane proteins are intimately linked to the properties of the membrane environment in which the proteins are embedded. For structural and biophysical characterization, membrane proteins generally need to be extracted from the membrane and reconstituted in a suitable membrane-mimicking environment. Ensuring functional and structural integrity in these environments is often a major concern. The styrene/maleic acid co-polymer has recently been shown to be able to extract lipid/membrane protein patches directly from native membranes to form nanosize discoidal proteolipid particles, also referred to as native nanodiscs. In this work, we show that high-resolution solid-state NMR spectra can be obtained from an integral membrane protein in native nanodiscs, as exemplified by the 2x34kDa bacterial cation diffusion facilitator CzcD.
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