Moving HRPF to in-cell and in-vivo Applications

ABSTRACT

In-cell and in vivo hydroxyl radical protein footprinting (FPOP) enables studying protein structure and interactions directly within cells or live organisms, crucial for understanding molecular crowding’s effects. The method, using UV lasers to split hydrogen peroxide, labels proteins in situ. Recent developments, including single-cell flow systems and the PIXI platform, increase throughput and enable analysis of complex models like 3D cultures.

SPEAKER

In the Department of Chemistry and Biochemistry at UCSD, the Jones Lab is a structural proteomics group that uses biochemical, analytical, and biophysical approaches to study protein interactions important in biological processes. Their research focuses on protein footprinting methods coupled with mass spectrometry to identify these interactions. A major focus of their lab is extending FPOP as an in-cell method for monitoring proteins in their native cellular environment. This method would be especially useful for membrane proteins, the largest class of drug targets, which are challenging to study in vitro owing to the difficulty of purifying these proteins. The Jones lab has further expanded FPOP for in vivo analysis in C. elegans, an animal model for human disease.

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