Issue 85, 2015
From the journal:

Chemical Communications

Controlling release, unfolding and dissociation of membrane protein complexes in the gas phase through collisional cooling†

Michael Landreh,a   Idlir Liko,a   Povilas Uzdavinys,b   Mathieu Coincon,b   Jonathan T. S. Hopper,a   David Drewb  and  Carol V. Robinson*a  

* Corresponding authors

a Department of Chemistry, Theoretical and Physical Chemistry Laboratory, University of Oxford, Oxford OX1 3TA, UK
E-mail: Carol.Robinson@chem.ox.ac.uk

b Centre for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden

Abstract

Mass spectrometry of intact membrane protein complexes requires removal of the detergent micelle by collisional activation. We demonstrate that the necessary energy can be obtained by adjusting the degree of collisional cooling in the ion source. This enables us to extend the energy regime for dissociation of membrane protein complexes.

Graphical abstract: Controlling release, unfolding and dissociation of membrane protein complexes in the gas phase through collisional cooling

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Article information

DOI
https://doi.org/10.1039/C5CC07045G
Article type
Communication
Submitted
21 Aug 2015
Accepted
03 Sep 2015
First published
03 Sep 2015

Chem. Commun., 2015,51, 15582-15584

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Controlling release, unfolding and dissociation of membrane protein complexes in the gas phase through collisional cooling

M. Landreh, I. Liko, P. Uzdavinys, M. Coincon, J. T. S. Hopper, D. Drew and C. V. Robinson, Chem. Commun., 2015, 51, 15582 DOI: 10.1039/C5CC07045G

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