BYU

Abstract by Austin Jarrett

Personal Infomation


Presenter's Name

Austin Jarrett

Degree Level

Undergraduate

Abstract Infomation


Department

Physics and Astronomy

Faculty Advisor

Dennis Della Corte

Title

Redesign of Radical SAM Enzyme

Abstract

The radical S-adenosyl-L-methionine (SAM) enzyme superfamily catalyzes a wide variety of biochemical reactions, usually through formation of a radical intermediate. Redesign of SAM enzymes yields a promising path to create novel biocatalysts. To engineer a protein with novel enzymatic functionality, sequential mutations were made to existing proteins using a computational multi-state design. Various radical SAM enzyme structures were analyzed for use as a protein scaffold using Rosetta and were evaluated with protein-substrate interactions using molecular dynamics simulations. Following completion of this design in silico, the protein will be synthesized in vitro. This protein is expected to be capable of catalyzing reactions that were previously difficult, hazardous, or expensive to carry out. Multi-state design promises to revolutionize the chemical and pharmaceutical industries.