Ontology highlight
ABSTRACT:
SUBMITTER: Lemmon G
PROVIDER: S-EPMC3342459 | biostudies-other | 2012 Jun
REPOSITORIES: biostudies-other
Lemmon Gordon G Kaufmann Kristian K Meiler Jens J
Chemical biology & drug design 20120319 6
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 is less sensitive to mutation. Thereby the HIV-1 protease/inhibitor binding affinity ...[more]