B.S. (Louisiana State University, USA, 2002)
Ph.D. (University of Texas, Austin, USA, 2010)
Postdoc (University of Illinois, Urbana-Champaign, USA, 2011-2016)
Office: Otto Maass 222
Phone: (514) 398-3637
Lab: P&P 312
Email: Christopher.Thibodeaux [at] McGill.ca
Webpage: Thibodeaux Group Website
Our research applies a diverse set of experimental tools spanning the realms of biochemistry, analytical chemistry, biophysics, molecular biology, and bioinformatics to study the biosynthesis of antimicrobial natural products, the biological processes that contribute to bacterial virulence, and the role of protein conformational dynamics in enzymes of biomedical relevance to humans.
Correlating Structure with Function in Enzymes of Biomedical Relevance
Broadly, we are interested in understanding the mechanisms of natural product biosynthetic enzymes and in understanding the role of protein conformational changes and structural dynamics in enzyme function. Many of our projects focus on enzymes that make antimicrobial compounds, that contribute to bacterial virulence/pathogenesis, or that have other biomedically-relevant functions. In general, the enzymes we study also rely on conformational changes to facilitate substrate recognition, signal with other enzymes, mediate allosteric activation, or to define the kinetic and catalytic properties of the enzyme. Our research employs a range of methodologies that provide trainees with a diverse experimental tool kit for careers in academia, private industry, or medicine. This includes expertise in molecular biology, biochemistry, microbiology, bioinformatics, analytical chemistry, quantitative analysis and data fitting, as well as biophysics and structural modelling. In particular, we have strong interests in the application of emerging mass spectrometry-based techniques and other biophysical approaches to correlate enzyme structural dynamics with biochemical functions.