BEGIN:VCALENDAR VERSION:2.0 PRODID:-//132.216.98.100//NONSGML kigkonsult.se iCalcreator 2.20.4// BEGIN:VEVENT UID:20250821T045230EDT-7135v1ibEZ@132.216.98.100 DTSTAMP:20250821T085230Z DESCRIPTION:Abstract:\n\nEnzymes are structurally dynamic molecules that pl ay essential roles in many processes related to human health and disease. Despite the recognition for many years that enzyme structural transitions (conformational changes) are integral to the biochemical function and regu lation of enzymes\, the precise relationships between enzyme conformation and function are often incompletely understood. A better understanding of the structural dynamic mechanisms of enzyme function could inform applicat ions in drug development\, synthetic biology\, or the engineering of enzym es with new functions. My group has been interested in the conformational dynamic properties of enzymes in several contexts that are relevant to hum an health and disease. First\, we have investigated the lanthipeptide synt hetase enzymes that install multiple thioether macrocycles into geneticall y encoded peptide antibiotics. Despite their relaxed substrate specificity \, these enzymes often manage to install sets of thioether rings with prec ise control over the regio- and stereoselectivity of the macrocyclization. By making innovative use of a suite of mass spectrometry-based approaches \, my group has begun to untangle the complex relationships between struct ural dynamics\, conformational changes\, and biochemical function in lanth ipeptide synthetases. We are currently expanding this pioneering work on l anthipeptide synthetases to investigate the conformational dynamic propert ies of other natural product biosynthetic enzymes\, and to develop and ada pt additional biophysical measurements with improved spatial and temporal resolution. Second\, in collaboration with the Auclair group\, we have aga in turned to mass spectrometry to investigate the structural basis of allo steric regulation in cytochrome P450 enzymes\, which play an essential rol e in drug metabolism in humans. The data show that P450 enzymes are confor mational chameleons\, whose structure and function are determined in part by the identity and location of the bound ligand. Future work will shift t o investigating the reductase enzyme that regulates P450 activity through dynamic protein-protein interactions. Cumulatively\, these and other effor ts by my group have illustrated the unique ability of biological mass spec trometry to reveal previously intractable mechanistic information on confo rmationally dynamic enzymes of relevance to human health and disease.\n\n  \n\nBio:\n\nChristopher J. Thibodeaux is a native of Louisiana (USA)\, whe re he graduated valedictorian with bachelor's degrees in Biochemistry\, Bo tany\, and Chemistry from Louisiana State University. He then entered grad uate school in the lab of Hung-wen Liu at the University of Texas\, Austin \, where his Ph.D. focused on elucidating the chemical and kinetic mechani sms of enzyme catalysis. Following graduation\, he completed postdoctoral stints in the labs of Taekjip Ha and Wilfred van der Donk at the Universit y of Illinois\, Urbana-Champaign\, where he studied biomolecular single mo lecule fluorescence spectroscopy and peptide natural product biosynthesis\ , respectively. In 2016\, he began his independent career in at Â鶹ɫÇéƬ Uni versity\, where he is currently an Assistant Professor in the Department o f Chemistry and the Associate Director of the Â鶹ɫÇéƬ Centre de Recherche e n Biologie Structurale. His research is broadly aimed at combatting the pr oblem of antimicrobial resistance by understanding the detailed molecular mechanisms of enzymes that synthesize structurally complex antimicrobial c ompounds\, discovering novel antimicrobial compounds by genome mining\, an d by investigating the molecular mechanisms of bacterial virulence. In his spare time\, he enjoys the outdoors\, cooking and eating spicy food\, lar ge family gatherings\, watching (American) football and baseball\, and spe nding time with his wife and three daughters.\n\n \n DTSTART:20221108T180000Z DTEND:20221108T193000Z LOCATION:Room 10\, Maass Chemistry Building\, CA\, QC\, Montreal\, H3A 0B8\ , 801 rue Sherbrooke Ouest SUMMARY:Chemical Society Seminar: Christopher Thibodeaux- Correlating Form and Function in Enzymes Related to Health and Disease URL:/chemistry/channels/event/chemical-society-seminar -christopher-thibodeaux-correlating-form-and-function-enzymes-related-heal th-343281 END:VEVENT END:VCALENDAR