Broadly, research in our lab is centered in mechanistic enzymology, natural product biosynthesis, and protein biophysics. We are interested in understanding the mechanisms of natural product biosynthetic enzymes and in understanding the role of protein conformational changes (i.e. molecular motions) and structural dynamics in enzyme function. Many of our projects focus on enzymes that construct antimicrobial compounds, that contribute to bacterial virulence/pathogenesis, or that have other biomedically-relevant functions. Thus, our research seeks to elucidate biological mechanisms that are highly relevant to drug development and human health. In general, the enzymes we study rely on conformational changes to facilitate substrate recognition, mediate allosteric activation, or to define the kinetic and catalytic properties of the enzyme. We employ specialized, emerging biophysical measurements to examine these functionally important enzyme molecular motions. Our research employs a range of methodologies encompassing molecular biology, biochemistry, microbiology, bioinformatics, analytical chemistry, quantitative analysis, data fitting, biophysics, and structural modelling. In particular, we have strong interests in the application of mass spectrometry-based techniques and other biophysical approaches to correlate enzyme structural dynamics with biochemical functions. Follow the links below to learn more about some of the on-going projects in our lab.
Biomolecular Mass Spectrometry
Mechanistic Enzymology of RiPP Biosynthesis
The Thibodeaux Lab 