Friday, August 7, 2020, 12:00 pm — ZoomGov
X-ray footprinting (XFP) is a tried-and-true method for probing macromolecule structure in solution. In XFP, hydroxyl radicals produced by X-ray radiolysis covalently label protein side chains and cleave phosphodiester backbones of nucleic acids, providing insight into macromolecular structure and dynamics that complements data obtained from crystallography, cryo-EM, and small-angle X-ray scattering.
XFP beamline (17-BM) at NSLS-II uniquely provides unmatched photon flux density and high level of automation to help resolve challenging biophysical questions, not obtainable by other structural probes. Recent developments in mass spectrometry have advanced the structural analysis and can provide detailed sub-peptide and residue level information for protein footprinting studies. In this talk, we will illustrate the use of synchrotron X-ray footprinting technique for studying structural changes in KIN10 enzyme, a key plant metabolic enzyme, after binding to its phosphorylated disaccharide ligand.
Hosted by: Ignace Jarrige
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