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1 H High‐Resolution Magic Angle Spinning NMR Spectroscopy for the Investigation of a Ras Lipopeptide in a Lipid Membrane
Author(s) -
Huster Daniel,
Kuhn Karsten,
Kadereit Dieter,
Waldmann Herbert,
Arnold Klaus
Publication year - 2001
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 - 10.1002/1521-3773(20010316)40:6<1056::aid-anie10560>3.0.co;2-7
Subject(s) - magic angle spinning , peptide , lipid bilayer , chemistry , nuclear magnetic resonance spectroscopy , spectroscopy , membrane , lipopeptide , crystallography , biophysics , biochemistry , stereochemistry , physics , biology , quantum mechanics , bacteria , genetics
A double lipid‐modified peptide which mimics the seven amino acids of the C terminus of the N‐Ras protein has been investigated by high‐resolution 1 H magic angle spinning NMR spectroscopy. The axially symmetric motion of the peptide in the bilayer decreases the NMR line widths, which facilitates signal assignment and localization of the peptide in the membrane. The peptide is located in the lipid/water interface of the lipid membrane (see schematic representation).