Recent advances in protein engineering have allowed for the targeted modification of enzymes toward a desired application. In this study, we analyze diverse enzymes using computational methods and reveal trends relating to activity, stability, and selectivity. We compare crystal structures of wild type and mutant enzymes for which the activity and thermostability rates have been previously measured. Using a variety of common computational methods such as molecular dynamics (MD) simulations, docking, principal component analysis (PCA) clustering, protein structure prediction, and qualitative structural analysis, we investigated the extent to which these tools are able to yield effective predictions in enzyme design. This resulted in the development of an enzyme design dataset used to identify common themes of various enzyme design methods. We believe these findings will prove useful in helping those in the field of computational biochemistry and biophysics to evaluate existing tools and consider their effectiveness in more powerful enzyme design.

Trends in enzyme design derived from computational analysis

ACS Spring 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.