Analysis of conformational stability of interacting residues in protein binding interfaces.

ABSTRACT: After approximately 60 years of work, the protein folding problem has recently seen rapid advancement thanks to the inventions of AlphaFold and RoseTTAFold, which are machine-learning algorithms capable of reliably predicting protein structures from their sequences. A key component in their success was the inclusion of pairwise interaction information between residues. As research focus shifts towards developing algorithms to design and engineer binding proteins, it is likely that knowledge of interaction features at protein interfaces can improve predictions. Here, 574 protein complexes were analyzed to identify the stability features of their pairwise interactions, revealing that interactions between pre-stabilized residues are a selected feature in protein binding interfaces. In a retro

SUBMITTER: Chauhan VM 

PROVIDER: S-EPMC10681001 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature