Mass spectrometry tools for analysis of intermolecular interactions
AuthorsAuclair, Jared R.
Green, Karin M.
Evans, James E.
Schiffer, Celia A.
Petsko, Gregory A.
Agar, Jeffrey N.
UMass Chan AffiliationsDepartment of Biochemistry and Molecular Pharmacology
Department of Pediatrics
Document TypeBook Chapter
Biochemistry, Biophysics, and Structural Biology
Pharmacology, Toxicology and Environmental Health
MetadataShow full item record
AbstractThe 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.
Methods Mol Biol. 2012;896:387-98. Link to article on publisher's site
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/26024