Computational & Applied Mathematics & Statistics Events
[PAST EVENT] Cheminar: IM-MS Tools for the Characterization and Differentiation of Protein Samples
Location
Integrated Science Center (ISC), Room 1127540 Landrum Dr
Williamsburg, VA 23185Map this location
Cheminar by Theresa Gozzo '18, Research Assistant & PhD Candidate, University of Washington - Seattle
IM-MS Tools for the Characterization and Differentiation of Protein Samples
Monoclonal antibodies form the basis of a swiftly growing class of therapeutics. In contrast to traditional small molecule drugs, antibodies are large, flexible proteins generated from a biological source. Their heterogeneity and complexity pose challenges to study via traditional structural biology techniques; therefore, gas-phase approaches have been leveraged to characterize and differentiate them. Two approaches will be presented that can help characterize the structures of antibodies as well as distinguish similar antibodies from each other. First, a combination of solution conditions, charge reduction via Cation-to-Anion Proton-Transfer Reactions (CAPTR), and energy-dependent ion mobility-mass spectrometry (IM-MS) experiments were used to distinguish between IgG1 and IgG4. Second, online, temperature-controlled disulfide reduction will be introduced to showcase its potential for rapid characterization of IgG disulfide bond connectivity.
Theresa Gozzo obtained her bachelor’s degree in chemistry from William & Mary under the advisement of Dr. John C. Poutsma. After her introduction to proteomic research, she moved to Seattle to specialize in ion mobility-mass spectrometry of intact proteins in Dr. Matthew Bush’s lab at the University of Washington. She is currently a PhD candidate and will complete her degree in analytical chemistry in November 2023. Her research focuses on probing the effects of charge on gas-phase ion structures and increasing the information content of ion mobility experiments.
Friday, 29 September 3 - 4 pm ISC 1127
Refreshments served prior to presentation
Contact
[[chemistry]]