Native Mass Spectrometry as a Tool in Structural Biology

Kristina Lorenzen1, Esther van Duijn1

1 Utrecht University, Utrecht, The Netherlands
Publication Name:  Current Protocols in Protein Science
Unit Number:  Unit 17.12
DOI:  10.1002/0471140864.ps1712s62
Online Posting Date:  November, 2010
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Native mass spectrometry (native MS) gives information about the composition, topological arrangements, dynamics, and structural properties of protein complexes. The mass range is principally unlimited and highly dynamic, allowing the detection of small subunits and large complexes within the same measurement. The amount of protein needed for an analysis is, compared to most other structural biology methods, very low. This unit provides an introduction to native MS. It starts with an explanation of the basic method and details on how to measure intact proteins and protein complexes, and continues with the study of dynamics and complex stability in the gas phase. The final section discusses the most recent extension to the native MS field, ion mobility, which allows the direct assessment of the structural properties of the complexes of interest. Curr. Protoc. Protein Sci. 62:17.12.1‐17.12.17. © 2010 by John Wiley & Sons, Inc.

Keywords: native mass spectrometry; protein complex topology; structural biology; ion mobility–mass spectrometry; tandem mass spectrometry; sample preparation and conditions; protein ion charge states

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Table of Contents

  • Introduction
  • Generation of Ions
  • Mass Analyzers
  • Sample Requirements
  • Protein Ligand Binding
  • Specific or Non‐Specific Protein Complexes
  • Tandem Mass Spectrometry Experiments
  • Tandem MS to Study Membrane Proteins
  • In‐Solution Dissociation Experiments
  • Influencing Protein Charge States
  • Ion Mobility–Mass Spectrometry
  • Processing Structural Information
  • Summary
  • Acknowledgements
  • Literature Cited
  • Figures
  • Tables
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Literature Cited

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