PuSH - Publication Server of Helmholtz Zentrum München: Characterization of membrane proteins in isolated native cellular membranes by dynamic nuclear polarization solid-state NMR spectroscopy without purification and reconstitution.

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Jacso, T. ; Franks, W.T.* ; Rose, H.* ; Fink, U.* ; Broecker, J.* ; Keller, S.* ; Oschkinat, H.* ; Reif, B.

Characterization of membrane proteins in isolated native cellular membranes by dynamic nuclear polarization solid-state NMR spectroscopy without purification and reconstitution.

Angew. Chem.-Int. Edit. 51, 432-435 (2012)

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Open Access Green as soon as Postprint is submitted to ZB.

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Membrane proteins in their native cellular membranes are accessible by dynamic nuclear polarization magic angle spinning solid-state NMR spectroscopy without the need of purification and reconstitution (see picture). Dynamic nuclear polarization is essential to achieve the required gain in sensitivity to observe the membrane protein of interest.

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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

Keywords Membrane Proteins ; Nmr Spectroscopy ; Structural Biology ; Structure Elucidation; RESOLUTION

ISSN (print) / ISBN 1433-7851

e-ISSN 1521-3773

Journal Angewandte Chemie - Internationale Edition

Quellenangaben Volume: 51, Issue: 2, Pages: 432-435

Publisher Wiley

Publishing Place Weinheim

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Institute of Structural Biology (STB)