Improving the Accuracy of Protein Thermostability Predictions for Single Point Mutations.

ABSTRACT: Accurately predicting the protein thermostability changes upon single point mutations in silico is a challenge that has implications for understanding diseases as well as industrial applications of protein engineering. Free energy perturbation (FEP) has been applied to predict the effect of single point mutations on protein stability for over 40 years and emerged as a potentially reliable prediction method with reasonable throughput. However, applications of FEP in protein stability calculations in industrial settings have been hindered by a number of limitations, including the inability to model mutations to and from prolines in which the bonded topology of the backbone is modified and the complexity in modeling charge-changing mutations. In this study, we have extended the FEP+ protocol

SUBMITTER: Duan J 

PROVIDER: S-EPMC7335905 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature