|Biochimica et biophysica acta (2007) 1774:1604-13|
|New York Consortium on Membrane Protein Structure|
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The extraordinary efficiency and selectivity of potassium channels have made them ideal systems for biophysical and functional studies of ion conduction. ...
We carried out solid-state NMR studies of the selectivity filter region of the protein. Partial site-specific assignments of the NMR signals were obtained based on high field multidimensional solid-state NMR spectra of uniformly (13)C, (15)N enriched KcsA potassium channel from Streptomyces lividans. Both backbone and sidechain atoms were assigned for residues V76-D80 and P83-L90, in and near the selectivity filter region of the protein; this region exhibits good dispersion and useful chemical shift fingerprints. This study will enable structure, dynamic and mechanistic studies of ion conduction by NMR.
|Amino Acid Sequence Molecular Sequence Data Protein Structure, Secondary Bacterial Proteins Carbon Isotopes Magnetic Resonance Spectroscopy Potassium Channels Streptomyces lividans |
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