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Bicelle‐Enabled Structural Studies on a Membrane‐Associated Cytochrome b 5 by Solid‐State MAS NMR Spectroscopy
Author(s) -
Xu Jiadi,
Dürr Ulrich H. N.,
Im SangChoul,
Gan Zhehong,
Waskell Lucy,
Ramamoorthy Ayyalusamy
Publication year - 2008
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.200801338
Subject(s) - model lipid bilayer , chemistry , nuclear magnetic resonance spectroscopy , spectroscopy , membrane , solid state nuclear magnetic resonance , domain (mathematical analysis) , crystallography , analytical chemistry (journal) , lipid bilayer , nuclear magnetic resonance , stereochemistry , biochemistry , chromatography , physics , mathematics , quantum mechanics , lipid bilayer phase behavior , mathematical analysis
Spinning bicelles : Solving 3D structures of membrane proteins is a great challenge because of the difficulty in finding well‐behaved model membranes. Bicelles are well suited to overcome these difficulties and enable the use of solid‐state MAS NMR spectroscopy experiments for studies on a large soluble domain containing a low concentration of membrane protein cytochrome b 5 at 37 °C.