Accessible Requires Authentication Published by De Gruyter July 14, 2015

Extending native mass spectrometry approaches to integral membrane proteins

Albert Konijnenberg, Jeroen F. van Dyck, Lyn L. Kailing and Frank Sobott
From the journal Biological Chemistry


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.

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:


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Received: 2015-3-1
Accepted: 2015-7-6
Published Online: 2015-7-14
Published in Print: 2015-9-1

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