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Prediction of HIV-1 Protease/Inhibitor Affinity using RosettaLigand

Predicting HIV-1 protease/inhibitor binding affinity as the difference between the free energy of the inhibitor bound and unbound state remains difficult as the unbound state exists as an ensemble of conformations with various degrees of flap opening. We improve computational prediction of protease/...

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Main Authors: Lemmon, Gordon, Kaufmann, Kristian, Meiler, Jens
Formato: Artigo
Idioma:Inglês
Publicado: 2012
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC3342459/
https://ncbi.nlm.nih.gov/pubmed/22321894
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1111/j.1747-0285.2012.01356.x
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