title: Characterization of membrane proteins in isolated native cellular membranes by dynamic nuclear polarization solid-state NMR spectroscopy without purification and reconstitution.
abstract: 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.
authors: Helmholtz-Zentrum München (HMGU), Deutsches Forschungszentrum für Gesundheit und Umwelt, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany.
authors: Tomas
authors: T
authors: Jacso
authors: W Trent
authors: WT
authors: Franks
authors: Honor
authors: H
authors: Rose
authors: Uwe
authors: U
authors: Fink
authors: Jana
authors: J
authors: Broecker
authors: Sandro
authors: S
authors: Keller
authors: Hartmut
authors: H
authors: Oschkinat
authors: Bernd
authors: B
authors: Reif
mesh_terms: D002462:Cell Membrane / Q000737:chemistry; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000032:analysis*; D008565:Membrane Proteins / Q000032:analysis*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*
chemical_list: D029968:Escherichia coli Proteins; D008565:Membrane Proteins