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Heteronuclear Multidimensional NMR Spectroscopy of Solubilized Membrane Proteins: Resonance Assignment of Native Bacteriorhodopsin
Author(s) -
Schubert Mario,
Kolbe Michael,
Kessler Brigitte,
Oesterhelt Dieter,
Schmieder Peter
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20021004)3:10<1019::aid-cbic1019>3.0.co;2-c
Subject(s) - bacteriorhodopsin , heteronuclear molecule , nuclear magnetic resonance spectroscopy , solubilization , chemistry , membrane protein , spectroscopy , nuclear magnetic resonance , biophysics , membrane , biochemistry , stereochemistry , biology , physics , quantum mechanics
Unraveling the loops : Use of recently developed NMR spectroscopy techniques can provide information about the loop regions that connect the transmembrane helices of membrane proteins such as G‐protein‐coupled receptors. A solution‐state NMR study of the native integral membrane protein bacteriorhodopsin is presented. Bacteriorhodopsin was used as a model system for proteins that consist of seven transmembrane helices. Experiments applied TROSY‐type NMR spectroscopy techniques to uniformly 2 H/ 15 N‐ and 2 H/ 13 C/ 15 N‐labeled samples solubilized with dodecylmaltoside. The assignment of 81 out of 248 residues, mainly in the loop regions, is given (see figure). Structural and dynamic information is derived from the data.