Electrostatic complementarity at the interface drives transient protein-protein interactions.

ABSTRACT: Understanding the mechanisms driving bio-molecules binding and determining the resulting complexes' stability is fundamental for the prediction of binding regions, which is the starting point for drug-ability and design. Characteristics like the preferentially hydrophobic composition of the binding interfaces, the role of van der Waals interactions, and the consequent shape complementarity between the interacting molecular surfaces are well established. However, no consensus has yet been reached on the role of electrostatic. Here, we perform extensive analyses on a large dataset of protein complexes for which both experimental binding affinity and pH data were available. Probing the amino acid composition, the disposition of the charges, and the electrostatic potential they generated on th

SUBMITTER: Grassmann G 

PROVIDER: S-EPMC10290103 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature