title: Controlling release, unfolding and dissociation of membrane protein complexes in the gas phase through collisional cooling.
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.
authors.affiliation: Department of Chemistry, Theoretical and Physical Chemistry Laboratory, University of Oxford, Oxford OX1 3TA, UK. Carol.Robinson@chem.ox.ac.uk.
authors.forename: Michael
authors.initials: M
authors.lastname: Landreh
authors.forename: Idlir
authors.initials: I
authors.lastname: Liko
authors.forename: Povilas
authors.initials: P
authors.lastname: Uzdavinys
authors.forename: Mathieu
authors.initials: M
authors.lastname: Coincon
authors.forename: Jonathan T S
authors.initials: JT
authors.lastname: Hopper
authors.forename: David
authors.initials: D
authors.lastname: Drew
authors.forename: Carol V
authors.initials: CV
authors.lastname: Robinson
mesh_terms: D005740:Gases / Q000737:chemistry; D013058:Mass Spectrometry; D008565:Membrane Proteins / Q000737:chemistry*; D058767:Protein Unfolding; D013816:Thermodynamics
chemical_list: D005740:Gases; D008565:Membrane Proteins