Source:http://linkedlifedata.com/resource/pubmed/id/11597403
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
21
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pubmed:dateCreated |
2001-10-12
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pubmed:abstractText |
Monte Carlo/free energy perturbation (MC/FEP) calculations were used to evaluate the binding free energy change for HIV-RT/inhibitor complexes upon L100I mutation. Inhibitor size and flexibility adjacent to hydrogen-bonding sites are evident as important considerations for antiviral drug design.
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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 |
Nov
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pubmed:issn |
0960-894X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2799-802
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading | |
pubmed:year |
2001
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pubmed:articleTitle |
Antiviral drug design: computational analyses of the effects of the L100I mutation for HIV-RT on the binding of NNRTIs.
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pubmed:affiliation |
Department of Chemistry, Yale University, New Haven, CT 06520, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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