Multiscale Computational Protocols for Accurate Residue Interactions at the Flexible Insulin-Receptor Interface.

ABSTRACT: The quantitative characterization of residue contributions to protein-protein binding across extensive flexible interfaces poses a significant challenge for biophysical computations. It is attributable to the inherent imperfections in the experimental structures themselves, as well as to the lack of reliable computational tools for the evaluation of all types of noncovalent interactions. This study leverages recent advancements in semiempirical quantum-mechanical and implicit solvent approaches embodied in the PM6-D3H4S/COSMO2 method for the development of a hierarchical computational protocols encompassing molecular dynamics, fragmentation, and virtual glycine scan techniques for the investigation of flexible protein-protein interactions. As a model, the binding of insulin to its receptor

SUBMITTER: Yurenko YP 

PROVIDER: S-EPMC12152935 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature