Li, Zixuan Moniz, Heather Wang, Shuo Ramiah, Annapoorani Zhang, Fuming Moremen, Kelley W. High Structural Resolution Hydroxyl Radical Protein Footprinting Reveals an Extended Robo1-Heparin Binding Interface* The much improved properties of this probe make carbene footprinting a viable method for rapid and accurate identification of protein binding sites utilizing benign, near-UV photoactivation. Using this methodology the location of a carbohydrate substrate was accurately mapped to the binding cleft of lysozyme, and in a more complex example, the interactions between a 100 kDa, multi-domain deubiquitinating enzyme, USP5 and a diubiquitin substrate were located to different functional domains. Here we present a differential protein footprinting technique employing an efficient photo-activated probe for use with mass spectrometry. Methods that employ sensitive analytical techniques such as mass spectrometry have the potential to provide valuable insights with very little material and on short time scales. The ability to detect protein complexes, and map their sites of binding, is crucial to understanding basic biology at the molecular level. Specific interactions between proteins and their binding partners are fundamental to life processes. Scott, Daniel Layfield, Robert Wright, Timothy G. Carbene footprinting accurately maps binding sites in protein-ligand and protein-protein interactions
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