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Native Mass Spectrometry for the Characterization of Structure and Interactions of Membrane Proteins

  • Jeroen F. van Dyck
  • Albert Konijnenberg
  • Frank Sobott
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 1635)

Abstract

Over the past years, native mass spectrometry and ion mobility have grown into techniques that are widely applicable to the study of aspects of protein structure. More recently, it has become apparent that this approach provides a very promising avenue for the investigation of integral membrane proteins in lipid or detergent environments.

In this chapter, we discuss applications of native mass spectrometry and ion mobility in membrane protein research—what is important to take into consideration when working with membrane proteins, and what the requirements are for sample preparation for native mass spectrometry. Furthermore, we will discuss the types of information provided by the measurements, including the oligomeric state, subunit composition and stoichiometry, interactions with detergents or lipids, conformational transitions, and the binding and structural effect of ligands and drugs.

Key words

Native mass spectrometry Ion mobility Membrane proteins Detergent micelles Lipids 

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Copyright information

© Springer Science+Business Media LLC 2017

Authors and Affiliations

  • Jeroen F. van Dyck
    • 1
  • Albert Konijnenberg
    • 1
  • Frank Sobott
    • 1
    • 2
    • 3
  1. 1.Biomolecular and Analytical Mass Spectrometry Group, Chemistry DepartmentUniversity of AntwerpAntwerpBelgium
  2. 2.Astbury Centre for Structural Molecular BiologyUniversity of LeedsLeedsUK
  3. 3.School of Molecular and Cellular BiologyUniversity of LeedsLeedsUK

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