Accounting for Solvation Correlation Effects on the Thermodynamics of Water Networks in Protein Cavities.

ABSTRACT: Macromolecular recognition and ligand binding are at the core of biological function and drug discovery efforts. Water molecules play a significant role in mediating the protein-ligand interaction, acting as more than just the surrounding medium by affecting the thermodynamics and thus the outcome of the binding process. As individual water contributions are impossible to measure experimentally, a range of computational methods have emerged to identify hydration sites in protein pockets and characterize their energetic contributions for drug discovery applications. Even though several methods model solvation effects explicitly, they focus on determining the stability of specific water sites independently and neglect solvation correlation effects upon replacement of clusters of water molecu

SUBMITTER: Barros EP 

PROVIDER: S-EPMC10052353 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature