Spatial organization of hydrophobic and charged residues affects protein thermal stability and binding affinity.

ABSTRACT: What are the molecular determinants of protein-protein binding affinity and whether they are similar to those regulating fold stability are two major questions of molecular biology, whose answers bring important implications both from a theoretical and applicative point of view. Here, we analyze chemical and physical features on a large dataset of protein-protein complexes with reliable experimental binding affinity data and compare them with a set of monomeric proteins for which melting temperature data was available. In particular, we probed the spatial organization of protein (1) intramolecular and intermolecular interaction energies among residues, (2) amino acidic composition, and (3) their hydropathy features. Analyzing the interaction energies, we found that strong Coulombic interac

SUBMITTER: Desantis F 

PROVIDER: S-EPMC9287411 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature