Auclair, Jared R.Somasundaran, MohanGreen, Karin M.Evans, James E.Schiffer, Celia A.Ringe, DagmarPetsko, Gregory A.Agar, Jeffrey N.2022-08-232022-08-232012-07-242012-10-10<p>Methods Mol Biol. 2012;896:387-98. <a href="http://dx.doi.org/10.1007/978-1-4614-3704-8_26" target="_blank">Link to article on publisher's site</a></p>1064-3745 (Linking)10.1007/978-1-4614-3704-8_2622821539https://hdl.handle.net/20.500.14038/26024The small quantities of protein required for mass spectrometry (MS) make it a powerful tool to detect binding (protein-protein, protein-small molecule, etc.) of proteins that are difficult to express in large quantities, as is the case for many intrinsically disordered proteins. Chemical cross-linking, proteolysis, and MS analysis, combined, are a powerful tool for the identification of binding domains. Here, we present a traditional approach to determine protein-protein interaction binding sites using heavy water ((18)O) as a label. This technique is relatively inexpensive and can be performed on any mass spectrometer without specialized software.en-USMass SpectrometryProtein BindingBinding SitesBiochemistry, Biophysics, and Structural BiologyMolecular BiologyPharmacology, Toxicology and Environmental HealthBook Chapterhttps://escholarship.umassmed.edu/bmp_pp/1533383248bmp_pp/153