Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs

Nils Hellwig; Oliver Peetz; Zainab Ahdash; Igor Tascón; Paula J. Booth; Vedrana Mikusevic; Marina Diskowski; Argyris Politis; Yvonne Hellmich; Inga Hänelt; Eamonn Reading; Nina Morgner

doi:10.1039/C8CC06284F

Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs†

Nils Hellwig,‡^a Oliver Peetz,‡^a Zainab Ahdash,^b Igor Tascón,

^c Paula J. Booth,^b Vedrana Mikusevic,^c Marina Diskowski,^c Argyris Politis,^b Yvonne Hellmich,^c Inga Hänelt,

^c Eamonn Reading

^b and Nina Morgner

*^a

Author affiliations

* Corresponding authors

^a Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt, Max-von-Laue-Straße 7, 60438 Frankfurt, Germany
E-mail: morgner@chemie.uni-frankfurt.de

^b Department of Chemistry, King's College London, 7 Trinity Street, London, UK

^c Institute of Biochemistry, Goethe University Frankfurt, Max-von-Laue-Straße 9, 60438 Frankfurt, Germany

Abstract

Other than more widely used methods, the use of styrene maleic acid allows the direct extraction of membrane proteins from the lipid bilayer into SMALPs keeping it in its native lipid surrounding. Here we present the combined use of SMALPs and LILBID-MS, allowing determination of oligomeric states of membrane proteins of different functionality directly from the native nanodiscs.

Chemical Communications

Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs†

Abstract

Supplementary files

Article information

Download Citation

Permissions

Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs

Social activity

Search articles by author

Spotlight

Advertisements