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Characterization of Membrane Proteins in Isolated Native Cellular Membranes by Dynamic Nuclear Polarization Solid‐State NMR Spectroscopy without Purification and Reconstitution
Author(s) -
Jacso Tomas,
Franks W. Trent,
Rose Honor,
Fink Uwe,
Broecker Jana,
Keller Sandro,
Oschkinat Hartmut,
Reif Bernd
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201104987
Subject(s) - magic angle spinning , solid state nuclear magnetic resonance , membrane , nuclear magnetic resonance spectroscopy , spectroscopy , chemistry , polarization (electrochemistry) , membrane protein , biophysics , nuclear magnetic resonance , materials science , analytical chemistry (journal) , chromatography , biochemistry , biology , physics , stereochemistry , quantum mechanics
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.