A topology-based network tree for the prediction of protein-protein binding affinity changes following mutation.

ABSTRACT: The ability to predict protein-protein interactions is crucial to our understanding of a wide range of biological activities and functions in the human body, and for guiding drug discovery. Despite considerable efforts to develop suitable computational methods, predicting protein-protein interaction binding affinity changes following mutation (ΔΔG) remains a severe challenge. Algebraic topology, a champion in recent worldwide competitions for protein-ligand binding affinity predictions, is a promising approach to simplifying the complexity of biological structures. Here we introduce element- and site-specific persistent homology (a new branch of algebraic topology) to simplify the structural complexity of protein-protein complexes and embed crucial biological information into topolo

SUBMITTER: Wang M 

PROVIDER: S-EPMC7223817 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature