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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1994-4-18
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pubmed:abstractText |
X-ray standing waves (XSW) have been used to study the topology of the protein cytochrome c, bound to a negatively charged model membrane and adsorbed at a metal surface. At the metal surface, cytochrome c forms an hexagonally close-packed monolayer. A similar packing arrangement is observed at the surface of a self-assembled lipid film on silver. The data suggest that cytochrome c maintains its native globular structure upon surface binding and subsequent storage for an extended period. Further, the data are consistent with a protein docking mechanism wherein the heme plane is oriented perpendicular to and with its exposed edge facing the surface. This study demonstrates the utility of XSW as a new and powerful structural tool for investigating membrane- and surface-protein interactions.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Selenomethionine,
http://linkedlifedata.com/resource/pubmed/chemical/Silver
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
237
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8133512-Adsorption,
pubmed-meshheading:8133512-Cytochrome c Group,
pubmed-meshheading:8133512-Fluorescence,
pubmed-meshheading:8133512-Membrane Proteins,
pubmed-meshheading:8133512-Proteins,
pubmed-meshheading:8133512-Selenomethionine,
pubmed-meshheading:8133512-Silver,
pubmed-meshheading:8133512-X-Rays
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pubmed:year |
1994
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pubmed:articleTitle |
Structure characterization of membrane bound and surface adsorbed protein.
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pubmed:affiliation |
Department of Chemistry, Ohio State University, Columbus 43210.
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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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