Enhancing Protein Purification Processes with Thermal Unfolding and Affinity Determination
Part of the BTEC Fall 2019 Seminar Series
Friday, Nov. 22, 2019
BTEC Room 135
Open to the public
The thermal stability of a protein is a key indicator of its physical stability, which in turn affects downstream processes. By monitoring protein stability with thermal unfolding and label-free differential scanning fluorimetry, protein quality can be assessed throughout the protein purification and characterization workflow to optimize conditions and ensure optimal performance. Functionality of purified proteins can be further interrogated by affinity assays such as microscale thermophoresis to determine its binding properties. Case studies that highlight these processes will be presented during the seminar.
Dinorah Leyva has a B.Sc. in Biomedical Research (Biochemistry) from the National Autonomous University of Mexico and a Ph.D. in Medical Sciences (Microbiology and Immunology) from Texas A&M University, where she studied the transcriptional response of immune cells to Shiga toxin. She was a postdoctoral fellow at the University of Texas at Austin, studying intracellular membrane trafficking and metal ion homeostasis. She joined NanoTemper Technologies as a Field Application Specialist in 2014 and is currently Senior Scientific Advisor.