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.

The authoritative guide to analyzing protein interactions by massspectrometryMass spectrometry (MS) is playing an increasingly important role inthe study of protein interactions. Mass Spectrometry of ProteinInteractionspresents timely and definitive discussions of thediverse range of approaches for studying protein interactions bymass spectrometry with an extensive set of references to theprimary literature. Each chapter is written by authors or teams ofauthors who are international authorities in their fields. Thisleading reference text:* Discusses the direct detection of protein interactions throughelectrospray ionization (ESI-MS); ion mobility analysis; andmatrix-assisted laser desorption/ionization (MALDI-MS)* Covers the indirect analysis of protein interactions throughhydrogen-deuterium exchange (HX-MS); limited proteolysis;cross-linking; and radial probe (RP-MS)* Guides researchers in the use of mass spectrometry in structuralbiology, biochemistry, and protein science to map and define thehuge number and diversity of protein interactions* Reviews the latest discoveries and applications and addresses newand ongoing challengesThis is a comprehensive reference for researchers in academia andindustry engaged in studies of protein interactions and anexcellent text for graduate and postgraduate students.

Preface.Contributors.Chapter 1. Direct Characterization of Protein Complexes byElectrospray 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 byMatrix-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 ProteinComplexes.2.4 Laser Fluence, Wavelength and Ion Extraction.2.5 Preservation of Protein Complexes on Conventional MaldiTargets.2.6 Affinity Targets and Surfaces Coupled To Maldi.2.7 Conclusions.Chapter 3. Probing Protein Interactions UsingHydrogen-Deuterium Exchange Mass Spectrometry (David D. Weis, SumaKaveti, 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 ProteinComplexes (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 forInvestigation of Protein-Protein Interactions (AndreaSinz).Introduction.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 MassSpectrometry (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 SpectrometryExperiments.6.4 Generation of Radicals on Millisecond Timescales.6.5 Applications of RP-MS to Studies of ProteinInteractions.6.6 Onset of Oxidative Damage and Its Implications for ProteinInteractions.6.7 Application of Radical Oxidation to Study ProteinAssemblies.6.8 Modeling Protein Complexes with Data from RP-MSExperiments.6.9 Conclusions.Index.