Source:http://linkedlifedata.com/resource/pubmed/id/17974509
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
2007-12-17
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pubmed:abstractText |
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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1774
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1604-13
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pubmed:meshHeading |
pubmed-meshheading:17974509-Amino Acid Sequence,
pubmed-meshheading:17974509-Bacterial Proteins,
pubmed-meshheading:17974509-Carbon Isotopes,
pubmed-meshheading:17974509-Magnetic Resonance Spectroscopy,
pubmed-meshheading:17974509-Molecular Sequence Data,
pubmed-meshheading:17974509-Potassium Channels,
pubmed-meshheading:17974509-Protein Structure, Secondary,
pubmed-meshheading:17974509-Streptomyces lividans
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pubmed:year |
2007
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pubmed:articleTitle |
Solid-state NMR study and assignments of the KcsA potassium ion channel of S. lividans.
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pubmed:affiliation |
Department of Chemistry, Columbia University, 3000 Broadway MC 3113, New York, NY 10027, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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