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American Chemical Society, Biochemistry, 20(49), p. 4297-4299, 2010

DOI: 10.1021/bi100031a

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Footprinting of Protein Interactions by Tritium Labeling

Journal article published in 2010 by Guillaume Mousseau, Quentin Raffy, Olivier P. Thomas, Morgane Agez, Robert Thai, Jean Philippe Renault ORCID, Serge Pin, Françoise Ochsenbein, Jean-Christophe Cintrat, Bernard Rousseau
This paper is available in a repository.
This paper is available in a repository.

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Abstract

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(122-135) and the protein hAsf1A(1-156) afforded data in good agreement with NMR results.