Mass spectrometry tools for analysis of intermolecular interactions.

TitleMass spectrometry tools for analysis of intermolecular interactions.
Publication TypeJournal Article
Year of Publication2012
AuthorsAuclair JR, Somasundaran M, Green KM, Evans JE, Schiffer CA, Ringe D, Petsko GA, Agar JN
JournalMethods Mol Biol
Date Published2012
KeywordsChromatography, Liquid, Cross-Linking Reagents, Electrophoresis, Polyacrylamide Gel, Mass Spectrometry, Peptides, Protein Binding, Protein Multimerization, Protein Structure, Quaternary, Protein Structure, Tertiary, Proteins, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Tandem Mass Spectrometry

The 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.

Alternate JournalMethods Mol. Biol.
PubMed ID22821539
Grant List1R21NS071256 / NS / NINDS NIH HHS / United States
GM 26788 / GM / NIGMS NIH HHS / United States
GM 32415 / GM / NIGMS NIH HHS / United States
P01 GM091743 / GM / NIGMS NIH HHS / United States
R21 A1067021 / / PHS HHS / United States