Journal of the American Chemical Society · 2008 · 82 citations · 64 references
Natural SciencesBiochemistryBiophysicsBiophysical ChemistryIon Channel BiophysicsMembrane BiophysicsChannel StructureIon Channel PhysiologyIon ChannelsIon SelectivityLipid Bilayer StructurePotassium Channel BiophysicsIon Channel SelectivityIon Channel StructureIon Channel Structure-function RelationshipsPotassium Channel DynamicsPotassium Channel GatingPotassium Channel PhysiologySolution-state SpectroscopyVoltage-gated Potassium Channels
We show that solid-state NMR can be used to investigate the structure and dynamics of a chimeric potassium channel, KcsA-Kv1.3, in lipid bilayers. Sequential resonance assignments were obtained using a combination of (15)N- (13)C and (13)C- (13)C correlation experiments conducted on fully labeled and reverse-labeled as well as C-terminally truncated samples. Comparison of our results with those from X-ray crystallography and solution-state NMR in micelles on the closely related KcsA K (+) channel provides insight into the mechanism of ion channel selectivity and underlines the important role of the lipid environment for membrane protein structure and function.
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Nuclear Magnetic Resonance Spectra from a Crystal rotated at High Speed
E.R. Andrew, A. Bradbury, R. G. Eades · Nature · 1958 · 1.2K citations
Natural Sciences, Physics, Radiology +13