SSIPe: accurately estimating protein-protein binding affinity change upon mutations using evolutionary profiles in combination with an optimized physical energy function.

ABSTRACT:

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 critical information for protein function annotation and genetic disease diagnoses.

Results

We present SSIPe, which combines protein interface profiles, collected from structural and sequence homology searches, with a physics-based energy function for accurate ΔΔGbind estimation. To offset the statistical limits of the PPI structure and sequence databases, amino acid-sp

SUBMITTER: Huang X 

PROVIDER: S-EPMC7178439 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature