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

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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 versatility for providing structural information about challenging biological macromolecules such as antibodie...

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Bibliographic Details
Call Number:Libro Electrónico
Other Authors: Weis, David D. (Editor)
Format: Electronic eBook
Language:Inglés
Published: Chichester, West Sussex : Wiley, 2016.
Subjects:
Proteins > Analysis.
Mass spectrometry.
Proteins > analysis
Mass Spectrometry > methods
Mass Spectrometry
Protéines > Analyse.
Spectrométrie de masse.
mass spectrometry.
SCIENCE > Life Sciences > Biochemistry.
Mass spectrometry
Proteins > Analysis
Online Access:Texto completo
Table of 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.

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