Source:http://linkedlifedata.com/resource/pubmed/id/12167032
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
32
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pubmed:dateCreated |
2002-8-8
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pubmed:abstractText |
Solid-state NMR spectroscopy, in conjunction with rigid body molecular dynamics calculations, shows that monomeric phospholamban in lipid bilayers has two distinct helical domains, with an interhelical angle within 60-100 degrees, ruling out the possibility of a continuous alpha-helical structure for this protein.
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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 |
Aug
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pubmed:issn |
0002-7863
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
124
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9392-3
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading | |
pubmed:year |
2002
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pubmed:articleTitle |
Solid-state NMR and rigid body molecular dynamics to determine domain orientations of monomeric phospholamban.
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pubmed:affiliation |
Department of Chemistry, University of Minnesota, Minneapolis 55455, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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