SpringerProtocols: Abstract: Protein Interactions Probed With Mass Spectrometry

Protein Interactions Probed With Mass Spectrometry

By: Suma Kaveti², John R. Engen³

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Understanding the interactions of proteins with other proteins and/or with drug molecules is essential for understanding the progression of diseases. In this chapter, we present several methods utilizing mass spectrometry (MS) for the analysis of protein-protein, protein-drug, and protein-metal interactions. We describe the analysis of protein interactions with hydrogen exchange MS methods. Hydrogen exchange methods can be used to analyze conformational changes on binding, to estimate dissociation constants, and to locate the sites of interaction/binding between binding partners. We also discuss more direct MS methods, including the analysis of metal ion complexation with proteins.

Affiliation(s): (2) Lerner Research Institute Proteomics Core, Cleveland Clinic foundation, Cleveland, OH
(3) Department of Chemistry, University of New Mexico, Albuquerque, NM

Book Title: Bioinformatics and Drug Discovery

Series: Methods in Molecular Biology | Volume: 316 | Pub. Date: Oct-01-2005 | Page Range: 179-197 | DOI: 10.1385/1-59259-964-8:179

Subject: Bioinformatics

Key Words: Hydrogen exchange - dissociation constant - conformational changes - mass spectrometry - deuterium

References

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