Target-template relationships in protein structure prediction and their effect on the accuracy of thermostability calculations.

ABSTRACT: Improving protein thermostability has been a labor- and time-consuming process in industrial applications of protein engineering. Advances in computational approaches have facilitated the development of more efficient strategies to allow the prioritization of stabilizing mutants. Among these is FEP+, a free energy perturbation implementation that uses a thoroughly tested physics-based method to achieve unparalleled accuracy in predicting changes in protein thermostability. To gauge the applicability of FEP+ to situations where crystal structures are unavailable, here we have applied the FEP+ approach to homology models of 12 different proteins covering 316 mutations. By comparing predictions obtained with homology models to those obtained using crystal structures, we have identified that l

SUBMITTER: Lihan M 

PROVIDER: S-EPMC9878467 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature