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Hydrogen exchange mass spectrometry of proteins : fundamentals, methods, and applications

Author: David D Weis
Publisher: Chichester, West Sussex : Wiley, 2016.
Edition/Format:   eBook : Document : EnglishView all editions and formats
Summary:

Hydrogen exchange mass spectrometry is widely recognized for its ability to probe the structure and dynamics of proteins. The application of this technique is becoming widespread due to its  Read more...

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Genre/Form: Electronic books
Additional Physical Format: Print version:
Hydrogen exchange mass spectrometry of proteins.
Chichester, West Sussex : John Wiley & Sons, Inc., 2016
(DLC) 2015018015
Material Type: Document, Internet resource
Document Type: Internet Resource, Computer File
All Authors / Contributors: David D Weis
ISBN: 9781118703694 1118703693 9781118703731 1118703731 9781118703748 111870374X 1118616499 9781118616499
OCLC Number: 908839035
Description: 1 online resource
Contents: Title Page --
Table of Contents --
List of Contributors --
Foreword --
Preface --
References --
A Note about Nomenclature --
References --
1 Hydrogen Exchange --
1.1 Isotopic Exchange and the Study of Protein Conformation and Dynamics --
1.2 Amide HX in Unstructured Polypeptides --
1.3 Amide HX in Folded Polypeptides --
References --
2 Hydrogen Exchange Mass Spectrometry Experimental Design --
2.1 Application of HX-MS for Protein Dynamics --
2.2 Factors Governing HX --
2.3 HX-MS Workflow --
2.4 Centroids and Data Analysis --
References. 3 Data Processing in Bottom-Up Hydrogen Exchange Mass Spectrometry --
3.1 Introduction --
3.2 The Deuterated Isotopic Distribution --
3.3 Essential Elements of an HX-MS Data Processing Workflow --
3.4 Select Software Packages for Automation of Analysis --
3.5 Ongoing and Future Challenges --
References --
4 Method Validation and Standards in Hydrogen Exchange Mass Spectrometry --
4.1 Introduction --
4.2 Rationale for a Reference Measurement System for HX-MS --
4.3 General Metrological Terminology --
4.4 Method Validation --
4.5 Standards: RM. 4.6 Summary: Maintaining Standards and Monitoring Performance --
References --
5 Millisecond Hydrogen Exchange --
5.1 Introduction --
5.2 Instrumentation --
5.3 Data Analysis --
5.4 Applications --
5.5 Conclusions and Outlook --
References --
6 Proteases for Hydrogen Exchange Mass Spectrometry --
6.1 Introduction --
6.2 The Use of Pepsin in HX-MS --
6.3 The Use of Other Commercially Available Proteases --
6.4 The Use of Other Acidic Proteases After Expression or Extraction --
References --
7 Extracting Information from Hydrogen Exchange Mass Spectrometry Data --
7.1 Introduction. 7.2 Basic Concepts in HX Data Analysis --
7.3 Algorithms for Extracting Rate Constants and Protection Factors --
7.4 Protein Dynamics Hidden in the Isotope Distributions --
7.5 Concluding Remarks and Future Prospects --
References --
8 Gas-Phase Fragmentation of Peptides to Increase the Spatial Resolution of the Hydrogen Exchange Mass Spectrometry Experiment --
8.1 Why Increase the Spatial Resolution in an HX Experiment Using MS/MS? --
8.2 H/D Scrambling in Peptides and How to Avoid It During MS/MS --
8.3 Integrating Gas-Phase Fragmentation Into the Classical Bottom-Up HX-MS Workflow. 8.4 Recent Applications of the Bottom-Up HX-MS/MS Workflow to Pinpoint the HX Properties of Proteins --
8.5 Future Directions --
References --
9 Top-Down Hydrogen Exchange Mass Spectrometry --
9.1 The Appeal of the Top-Down Scheme --
9.2 Top-Down HX-MS of Small Proteins: The Problem of Hydrogen Scrambling --
9.3 Conformer-Specific Characterization of Nonnative Protein States Using Top-Down HX ECD MS --
9.4 Convergence of Top-Down and Classical Schemes of HX-MS: Combination of Proteolytic and Gas-Phase Fragmentation without Chromatographic Separation.
Responsibility: edited by David D. Weis.

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