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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

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Volume 396, Issue 9-10

Issues

Extending native mass spectrometry approaches to integral membrane proteins

Albert Konijnenberg
  • Biomolecular and Analytical Mass Spectrometry group, Department of Chemistry, University of Antwerp, Antwerp, Belgium
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/ Jeroen F. van Dyck
  • Biomolecular and Analytical Mass Spectrometry group, Department of Chemistry, University of Antwerp, Antwerp, Belgium
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/ Lyn L. Kailing
  • Biomolecular and Analytical Mass Spectrometry group, Department of Chemistry, University of Antwerp, Antwerp, Belgium
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/ Frank Sobott
  • Corresponding author
  • Biomolecular and Analytical Mass Spectrometry group, Department of Chemistry, University of Antwerp, Antwerp, Belgium
  • UA-VITO Centre for Proteomics, University of Antwerp, Antwerp, Belgium
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  • Other articles by this author:
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Published Online: 2015-07-14 | DOI: https://doi.org/10.1515/hsz-2015-0136

Abstract

Recent developments in native mass spectrometry and ion mobility have made it possible to analyze the composition and structure of membrane protein complexes in the gas-phase. In this short review we discuss the experimental strategies that allow to elucidate aspects of the dynamic structure of these important drug targets, such as the structural effects of lipid binding or detection of co-populated conformational and assembly states during gating on an ion channel. As native mass spectrometry relies on nano-electrospray of natively reconstituted proteins, a number of commonly used lipid- and detergent-based reconstitution systems have been evaluated for their compatibility with this approach, and parameters for the release of intact, native-like folded membrane proteins studied in the gas-phase. The strategy thus developed can be employed for the investigation of the subunit composition and stoichiometry, oligomeric state, conformational changes, and lipid and drug binding of integral membrane proteins.

Keywords: detergent micelles; lipid binding; membrane proteins; native mass spectrometry; structural biology

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About the article

Corresponding author: Frank Sobott, Biomolecular and Analytical Mass Spectrometry group, Department of Chemistry, University of Antwerp, Antwerp, Belgium; and UA-VITO Centre for Proteomics, University of Antwerp, Antwerp, Belgium, e-mail:


Received: 2015-03-01

Accepted: 2015-07-06

Published Online: 2015-07-14

Published in Print: 2015-09-01


Citation Information: Biological Chemistry, Volume 396, Issue 9-10, Pages 991–1002, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/hsz-2015-0136.

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