Computational Assessment of Protein-protein Binding Affinity by Reversely Engineering the Energetics in Protein Complexes.

ABSTRACT: The cellular functions of proteins are maintained by forming diverse complexes. The stability of these complexes is quantified by the measurement of binding affinity, and mutations that alter the binding affinity can cause various diseases such as cancer and diabetes. As a result, accurate estimation of the binding stability and the effects of mutations on changes of binding affinity is a crucial step to understanding the biological functions of proteins and their dysfunctional consequences. It has been hypothesized that the stability of a protein complex is dependent not only on the residues at its binding interface by pairwise interactions but also on all other remaining residues that do not appear at the binding interface. Here, we computationally reconstruct the binding affinity by dec

SUBMITTER: Wang B 

PROVIDER: S-EPMC9403033 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature