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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1996-2-22
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pubmed:abstractText |
We propose a general mean field model of ligand-protein interactions to determine the thermodynamic equilibrium of a system at finite temperature. The method is employed in structural assessments of two human immuno-deficiency virus type 1 protease complexes where the gross effects of protein flexibility are incorporated by utilizing a data base of crystal structures. Analysis of the energy spectra for these complexes has revealed that structural and thermo-dynamic aspects of molecular recognition can be rationalized on the basis of the extent of frustration in the binding energy landscape. In particular, the relationship between receptor-specific binding of these ligands to human immunodeficiency virus type 1 protease and a minimal frustration principle is analyzed.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-1282717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-1304383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-1339024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-1409599,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-1480616,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-1509259,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-1557356,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-1603810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-17840193,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-1920412,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-1993177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-2046752,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-2075193,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-2201691,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-2217178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-2281083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-2300551,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-2388586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-2388698,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-3478708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-712840,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-7154081,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-7656055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-7724609,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-7784423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-7809158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-7932757,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8107095,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8114102,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8176736,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8183927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8196057,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8254666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8259000,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8289255,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8303294,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8309926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8346235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8352596,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8378312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8433368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8433976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8506353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-8514751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8552675-9383433
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
93
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
60-4
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
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pubmed:year |
1996
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pubmed:articleTitle |
A mean field model of ligand-protein interactions: implications for the structural assessment of human immunodeficiency virus type 1 protease complexes and receptor-specific binding.
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pubmed:affiliation |
Agouron Pharmaceuticals Inc., San Diego, CA 92121, USA.
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pubmed:publicationType |
Journal Article
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