Footprinting of Protein Interactions by Tritium Labeling Guillaume Mousseau Quentin Raffy Olivier P. Thomas Morgane Agez Robert Thai Jean Philippe Renault Serge Pin Françoise Ochsenbein Jean-Christophe Cintrat Bernard Rousseau 10.1021/bi100031a.s001 https://acs.figshare.com/articles/journal_contribution/Footprinting_of_Protein_Interactions_by_Tritium_Labeling/2767120 A new footprinting method for mapping protein interactions has been developed, using tritium as a radioactive label. As residues involved in an interaction are less labeled when the complex is formed, they can be identified via comparison of the tritium incorporation of each residue of the bound protein with that of the unbound one. Application of this footprinting method to the complex formed by the histone H3 fragment H3<sub>122−135</sub> and the protein hAsf1A<sub>1−156</sub> afforded data in good agreement with NMR results. 2010-05-25 00:00:00 tritium residue footprinting method protein hAsf 1A NMR mapping protein interactions