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The Role of the Detergent Micelle in Preserving the Structure of Membrane Proteins in the Gas Phase
Author(s) -
Reading Eamonn,
Liko Idlir,
Allison Timothy M.,
Benesch Justin L. P.,
Laganowsky Arthur,
Robinson Carol V.
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201411622
Subject(s) - micelle , chemistry , mass spectrometry , membrane , membrane protein , ion mobility spectrometry , ionization , ion , gas phase , phase (matter) , chromatography , analytical chemistry (journal) , organic chemistry , biochemistry , aqueous solution
Despite the growing importance of the mass spectrometry of membrane proteins, it is not known how their transfer from solution into vacuum affects their stability and structure. To address this we have carried out a systematic investigation of ten membrane proteins solubilized in different detergents and used mass spectrometry to gain physicochemical insight into the mechanism of their ionization and desolvation. We show that the chemical properties of the detergents mediate the charge state, both during ionization and detergent removal. Using ion mobility mass spectrometry, we monitor the conformations of membrane proteins and show how the surface charge density dictates the stability of folded states. We conclude that the gas‐phase stability of membrane proteins is increased when a greater proportion of their surface is lipophilic and is consequently protected by the physical presence of the micelle.