FPOP for Problem Solving in Protein Chemistry and Biology

ABSTRACT

FPOP has become a versatile tool in protein chemistry, offering microsecond-speed footprinting to track rapid protein folding and conformational changes, even those missed by slower techniques. It aids in epitope mapping, detects conformational changes in biopharmaceuticals, and studies protein-ligand interactions relevant to diseases like Alzheimer’s. FPOP is effective for membrane proteins and in living cells, providing unique insights. The lecture will compare FPOP with other footprinting methods.

SPEAKER

At Washington University in St. Louis, the Gross research group focuses mainly on the development of mass spectrometry (MS) in biophysics and structural proteomics, specifically to probe protein-ligand interaction interfaces, affinities, aggregation, and folding/unfolding. The work includes both instrument and method development and application to important proteins and protein complexes. His research group also employs specific chemical reagents to footprint proteins and determines their interfaces and orientations in complex biological settings, hydrogen/deuterium exchange, and native MS

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