Mass Spectrometry of Protein Interactions / Edition 1

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The authoritative guide to analyzing protein interactions by mass spectrometry

Mass spectrometry (MS) is playing an increasingly important role in the study of protein interactions. Mass Spectrometry of Protein Interactionspresents timely and definitive discussions of the diverse range of approaches for studying protein interactions by mass spectrometry with an extensive set of references to the primary literature. Each chapter is written by authors or teams of authors who are international authorities in their fields. This leading reference text:

Discusses the direct detection of protein interactions through electrospray ionization (ESI-MS); ion mobility analysis; and matrix-assisted laser desorption/ionization (MALDI-MS)

Covers the indirect analysis of protein interactions through hydrogen-deuterium exchange (HX-MS); limited proteolysis; cross-linking; and radial probe (RP-MS)

Guides researchers in the use of mass spectrometry in structural biology, biochemistry, and protein science to map and define the huge number and diversity of protein interactions

Reviews the latest discoveries and applications and addresses new and ongoing challenges

This is a comprehensive reference for researchers in academia and industry engaged in studies of protein interactions and an excellent text for graduate and postgraduate students.

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Product Details

  • ISBN-13: 9780471793731
  • Publisher: Wiley
  • Publication date: 8/24/2007
  • Series: Wiley Series on Mass Spectrometry Series, #26
  • Edition number: 1
  • Pages: 137
  • Product dimensions: 6.38 (w) x 9.53 (h) x 0.52 (d)

Meet the Author

Kevin M. Downard, PhD, is an Associate Professor in the School of Molecular and Microbial Biosciences at the University of Sydney in Australia. He has twenty years of research experience in mass spectrometry, with the past fifteen devoted to protein analysis.

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Table of Contents



Chapter 1. Direct Characterization of Protein Complexes by Electrospray Ionization Mass Spectrometry and Ion Mobility Analysis (Joseph A. Loo and Catherine S. Kaddis).

1.1 Introduction.

1.2 Critical Aspects of the Experimental Procedure.

1.3 Solution Phase Equilibria and Gas Phase Dissociation.

1.4 Conclusions.

Chapter 2. Softly, Softly-Detection of Protein Complexes by Matrix-Assisted Laser Desorption Ionisation Mass Spectrometry (Kevin M. Downard).

2.1 Introduction.

2.2 First Glimpses and the First-Shot Phenomenon.

2.3 Matrix and Solution Criteria to Preserve Protein Complexes.

2.4 Laser Fluence, Wavelength and Ion Extraction.

2.5 Preservation of Protein Complexes on Conventional Maldi Targets.

2.6 Affinity Targets and Surfaces Coupled To Maldi.

2.7 Conclusions.

Chapter 3. Probing Protein Interactions Using Hydrogen-Deuterium Exchange Mass Spectrometry (David D. Weis, Suma Kaveti, Yan Wu and John R. Engen).

3.1 Introduction.

3.2 Hydrogen Exchange Background.

3.3 General HX-MS Method.

3.4 Interactions of Proteins.

3.5 Examples.

3.6 Conclusions.

Chapter 4. Limited Proteolysis Mass Spectrometry of Protein Complexes (Maria Monti and Piero Pucci).

4.1 Introduction.

4.2 Limited Proteolysis Analysis.

4.3 Experimental Design.

4.4 Probing Protein-Protein Interactions.

4.5 Probing Protein-Nucleic Acid Interactions.

4.6 Protein-Ligand Interactions.

4.7 Probing Amyloid Fibril Core.

4.8 Conlusions.

Chapter 5. Chemical Cross-Linking and Mass Spectrometry for Investigation of Protein-Protein Interactions (Andrea Sinz).


5.1 Cross-Linking Strategies.

5.2 Functional Groups of Cross-Linking Reagents.

5.3 Mass Spectrometric Analysis of Cross-Linked Products.

5.4 Identification of Cross-Linked Produc.

5.5 Computer Software for Data Analysis.

5.6 Conclusions and Perspectives.

Chapter 6. Genesis & Application of Radical Probe Mass Spectrometry (RP-MS) to Study Protein Interactions (Simin D. Maleknia and Kevin M. Downard).

6.1 Genesis of Radical Probe Mass Spectrometry.

6.2 The Reactive Residue Side Chains.

6.3 Conditions Important to Radical Probe Mass Spectrometry Experiments.

6.4 Generation of Radicals on Millisecond Timescales.

6.5 Applications of RP-MS to Studies of Protein Interactions.

6.6 Onset of Oxidative Damage and Its Implications for Protein Interactions.

6.7 Application of Radical Oxidation to Study Protein Assemblies.

6.8 Modeling Protein Complexes with Data from RP-MS Experiments.

6.9 Conclusions.


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  • Anonymous

    Posted June 16, 2008

    A reviewer

    This new book is the first to be published on the subject and represents a timely and comprehensive review of the use of mass spectrometry to study protein interactions. Six chapters cover the direct use of ESI-MS and MALDI-MS to detect protein complexes and assemblies through to the coupling of hydrogen/deuterium exchange, limited proteolysis, chemical cross-linking, and radical probe mass spectrometry or radical oxidative footprinting to probe their structures. The book is a well written text by leaders in the field and documents the progress so far with many citations to the primary literatures. An excellent resource for graduate students, researchers, and academics interested in the area.

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  • Anonymous

    Posted October 20, 2008

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