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Article

Prediction of HIV-1 protease/inhibitor affinity using RosettaLigand.

Chemical biology & drug design - 1 Jun 2012

Lemmon Gordon, Kaufmann Kristian, Meiler Jens

Abstract excerpt

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/inhibitor affinity by invoking the hypothesis that the free energy of the unbound state while difficult to predict...

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Identifiers

PMID: 22321894
DOI: 10.1111/j.1747-0285.2012.01356.x
PMCID: PMC3342459

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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