Article
SSIPe: accurately estimating protein-protein binding affinity change upon mutations using evolutionary profiles in combination with an optimized physical energy function.
Bioinformatics (Oxford, England) - 15 Apr 2020
Huang Xiaoqiang, Zheng Wei, Pearce Robin, Zhang Yang
Abstract excerpt
MOTIVATION: Most proteins perform their biological functions through interactions with other proteins in cells. Amino acid mutations, especially those occurring at protein interfaces, can change the stability of protein-protein interactions (PPIs) and impact their functions, which may cause various human diseases. Quantitative estimation of the binding affinity changes (ΔΔGbind) caused by mutations can provide...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
