title: Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions.
abstract: We describe a general mass spectrometry approach to determine subunit stoichiometry and lipid binding in intact membrane protein complexes. By exploring conditions for preserving interactions during transmission into the gas phase and for optimally stripping away detergent, by subjecting the complex to multiple collisions, we released the intact complex largely devoid of detergent. This enabled us to characterize both subunit stoichiometry and lipid binding in 4 membrane protein complexes.
authors: Department of Chemistry, University of Cambridge, Cambridge, UK.
authors: Nelson P
authors: NP
authors: Barrera
authors: Shoshanna C
authors: SC
authors: Isaacson
authors: Min
authors: M
authors: Zhou
authors: Vassiliy N
authors: VN
authors: Bavro
authors: Alex
authors: A
authors: Welch
authors: Theresia A
authors: TA
authors: Schaedler
authors: Markus A
authors: MA
authors: Seeger
authors: Ricardo Núñez
authors: RN
authors: Miguel
authors: Vladimir M
authors: VM
authors: Korkhov
authors: Hendrik W
authors: HW
authors: van Veen
authors: Henrietta
authors: H
authors: Venter
authors: Adrian R
authors: AR
authors: Walmsley
authors: Christopher G
authors: CG
authors: Tate
authors: Carol V
authors: CV
authors: Robinson
mesh_terms: D026901:Membrane Transport Proteins / Q000737:chemistry*; D046912:Multiprotein Complexes / Q000737:chemistry*; D025941:Protein Interaction Mapping; D021122:Protein Subunits / Q000737:chemistry*; D040901:Proteomics / Q000379:methods*; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*
chemical_list: D026901:Membrane Transport Proteins; D046912:Multiprotein Complexes; D021122:Protein Subunits