Accelerated Hydration Site Localization and Thermodynamic Profiling.

ABSTRACT: Water plays a fundamental role in the structure and function of proteins and other biomolecules. The thermodynamic profile of water molecules surrounding a protein is critical for ligand recognition and binding. Therefore, identifying the location and thermodynamic properties of relevant water molecules is important for generating and optimizing lead compounds for affinity and selectivity for a given target. Computational methods have been developed to identify these hydration sites (HS), but are largely limited to simplified models that fail to capture multibody interactions or dynamics-based methods that rely on extensive sampling. Here, we present a method for fast and accurate localization and thermodynamic profiling of HS for protein structures. The method is based on a geometric deep

SUBMITTER: Hinz FB 

PROVIDER: S-EPMC11938278 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature