Examining the assumptions underlying continuum-solvent models.

ABSTRACT: Continuum-solvent models (CSMs) have successfully predicted many quantities, including the solvation-free energies (ΔG) of small molecules, but they have not consistently succeeded at reproducing experimental binding free energies (ΔΔG), especially for protein-protein complexes. Several CSMs break ΔG into the free energy (ΔGvdw) of inserting an uncharged molecule into solution and the free energy (ΔGel) gained from charging. Some further divide ΔGvdw into the free energy (ΔGrep) of inserting a nearly hard cavity into solution and the free energy (ΔGatt) gained from turning on dispersive interactions between the solute and solvent. We show that for 9 protein-protein complexes neither ΔGrep nor ΔGvdw was linear in the solvent-accessible area A, as assumed in many CSMs, and the corresponding

SUBMITTER: Harris RC 

PROVIDER: S-EPMC5340276 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature