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Mass Spectrometry of Protein Interactions. Wiley Series on Mass Spectrometry

  • ID: 2181429
  • Book
  • August 2007
  • 138 Pages
  • John Wiley and Sons Ltd
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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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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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Kevin Downard
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