Start: February 5, 2026 3:30 p.m.
End: February 5, 2026 4:30 p.m.
Exploration of Phosphoenolpyruvate Carboxykinases Using Integrative Structural Biology and Kinetics
Dr. Matt McLeod
Assistant Professor, Department of Chemistry, University of Cincinnati
Thursday, 2/05 @ 3:30 PM
FB 253
Enzymes are dynamic molecular scaffolds that adopt multiple conformations as they perform their function. To understand the role of protein dynamics in activity, the entire conformational sample under (near) native conditions should be observed. However, most structural biology projects collect data at cryogenic temperatures and often of a single static state. This approach yields a narrow view of the ensemble and precludes a comprehensive understanding of the structure-function relationship. An integrative approach using many methods, or novel methodologies that vary experimental parameters such as temperature or time, can produce a richer picture of enzyme dynamics. Here, three stories will be told. The first integrates various “traditional” structural methods to understand how evolved domains/lobes of an enzyme scaffold lead to allosteric regulation. The second shows structural data collected across a range of physiological temperatures, elucidating a mechanistic basis for temperature-induced increases in activity. The third introduces new instrumentation that enables researchers to observe enzymes in action. This method initiates reactions in crystals and quenches the reaction at defined time points, allowing a series of snapshots to be collected.