Ontology highlight
ABSTRACT:
SUBMITTER: Setny P
PROVIDER: S-EPMC2938831 | biostudies-other | 2010 Sep
REPOSITORIES: biostudies-other
Journal of chemical theory and computation 20100824 9
Hydrophobic association is often recognized as being driven by favorable entropic contributions. Here, using explicit solvent molecular dynamics simulations we investigate binding in a model hydrophobic receptor-ligand system which appears, instead, to be driven by enthalpy and opposed by entropy. We use the temperature dependence of the potential of mean force to analyze the thermodynamic contributions along the association coordinate. Relating such contributions to the ongoing changes in syste ...[more]