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Methods Mol Biol. 2012;896:387-98. doi: 10.1007/978-1-4614-3704-8_26.

Mass spectrometry tools for analysis of intermolecular interactions.

Author information

  • 1Department of Biochemistry and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA, USA. jared.auclair@gmail.com

Abstract

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.

PMID:
22821539
[PubMed - indexed for MEDLINE]
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