There is a profound need to determine structure and properties of proteins that do not crystallize and are not suitable for high-resolution NMR.  Most low-resolution approaches do not yield information at the peptide or amino-acid levels. Mass spectrometry (MS) coupled with chemical footprinting provides a means of determining protein interactions, following folding, and determining binding affinities and interaction sites. To this end, we are developing fast photochemical oxidation of proteins (FPOP) and implementing HD exchange (H/DX), and other covalent modifications to interrogate protein interactions, interfaces, and dynamics of folding/unfolding.  For irreversible labeling, we use FPOP, which has a significant advantage of speed, owing to the use of free radicals as footprinting reagents, and can be used to follow fast folding.  In the lecture, we will describe and provide context for these approaches, and outline some applications in protein science and structural biology.

Role of mass spectrometry-based protein footprinting in biophysics

245th National Meeting (2013)

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