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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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Autores principales: Lemmon, Gordon, Kaufmann, Kristian, Meiler, Jens
Formato: Artigo
Lenguaje:Inglês
Publicado: 2012
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Acceso en línea: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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