Ontology highlight
ABSTRACT:
SUBMITTER: Reynolds CH
PROVIDER: S-EPMC4018058 | biostudies-literature | 2011 Jun
REPOSITORIES: biostudies-literature
Reynolds Charles H CH Holloway M Katharine MK
ACS medicinal chemistry letters 20110323 6
Analysis of the experimental binding thermodynamics for approximately 100 protein-ligand complexes provides important insights into the factors governing ligand affinity and efficiency. The commonly accepted correlation between enthalpy and -TΔS is clearly observed for this relatively diverse data set. It is also clear that affinity (i.e., ΔG) is not generally correlated to either enthalpy or -TΔS. This is a worrisome trend since the vast majority of computational structure-based design is carri ...[more]