Source:http://linkedlifedata.com/resource/pubmed/id/10783287
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2000-7-19
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pubmed:abstractText |
Resonance patterns have been observed in 2D solid-state NMR spectra of the transmembrane segment of M2 protein from Influenza A virus in oriented samples reflecting the helical wheel of this alpha-helix. The center of this pattern uniquely defines the helical tilt with respect to the bilayer normal without a need for resonance assignments. The distribution of resonances from amino acid specific labels around the "PISA wheel" defines the rotational orientation of the helix and yields preliminary site-specific assignments. With assignments high-resolution structural detail, such as differences in tilt and rotational orientation along the helical axis leading to an assessment of helical coiling, can be obtained.
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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 |
May
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pubmed:issn |
1090-7807
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2000 Academic Press.
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pubmed:issnType |
Print
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pubmed:volume |
144
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
162-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10783287-Influenza A virus,
pubmed-meshheading:10783287-Lipid Bilayers,
pubmed-meshheading:10783287-Magnetic Resonance Spectroscopy,
pubmed-meshheading:10783287-Membrane Proteins,
pubmed-meshheading:10783287-Nitrogen Isotopes,
pubmed-meshheading:10783287-Protein Structure, Secondary
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pubmed:year |
2000
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pubmed:articleTitle |
Imaging membrane protein helical wheels.
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pubmed:affiliation |
National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida 32310, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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