Source:http://linkedlifedata.com/resource/pubmed/id/12069621
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2002-6-18
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pubmed:abstractText |
Ion channels are highly specific membrane-spanning protein structures which serve to facilitate the passage of selected ions across the lipid barrier. In the past decade, molecular dynamics simulations based on atomic models and realistic microscopic interactions with explicit solvent and membrane lipids have been used to gain insight into the function of these complex systems. These calculations have considerably expanded our view of ion permeation at the microscopic level. This Account will mainly focus on computational studies of the gramicidin A channel, one of the simplest and best characterized molecular pore.
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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 |
Jun
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pubmed:issn |
0001-4842
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
366-75
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pubmed:dateRevised |
2005-11-16
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pubmed:meshHeading | |
pubmed:year |
2002
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pubmed:articleTitle |
Computational studies of the gramicidin channel.
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pubmed:affiliation |
Department of Biochemistry, Weill Medical College of Cornell University, 1300 York Avenue, New York, New York 10021, USA. benoit.roux@med.cornell.edu
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pubmed:publicationType |
Journal Article,
Review
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