HRPF and its Relevance in Drug Development
ABSTRACT
In drug development, characterizing high-order structures (HOS) is essential for understanding protein functionality and stability. Hydroxy Radical Protein Footprinting (HRPF) is a powerful tool for revealing key aspects of protein HOS. It is used to map protein-protein and protein-ligand interactions, including antibody binding regions, aggregation sites, and the characterization of allosteric inhibitors. HRPF provides high-resolution insights while maintaining near-native protein conditions, making it a practical and accessible tool for optimizing therapeutic proteins.
SPEAKER
Dr. Emily Chea received her PhD while studying with Professor Dr. Lisa Jones at the University of Maryland, Baltimore. Emily has made significant contributions to the development of HRPF, with particular emphasis on in-cell FPOP (IC-FPOP) for proteome-wide structural biology characterization of cellular drug–target interactions. Currently, Emily is a key member of the GenNext scientific team in her role as an Applied Research Scientist Manager.
