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Here we examined the gas-phase structures of two tetrameric membrane protein complexes by ion mobility mass spectrometry. The collision cross sections measured for the ion channel are in accord with a compact configuration of subunits, suggesting that the native-like structure can be preserved under the harsh activation conditions required to release it from the detergent micelle into the gas phase. We also found that the quaternary structure of the transporter, which has fewer transmembrane subunits than the ion channel, is less stable once stripped of detergents and bulk water. These results highlight the potential of ion mobility mass spectrometry for characterizing the overall topologies of membrane protein complexes and the structural changes associated with nucleotide, lipid, and drug binding.

Original publication

DOI

10.1021/ja104312e

Type

Journal article

Journal

J Am Chem Soc

Publication Date

10/11/2010

Volume

132

Pages

15468 - 15470

Keywords

Gases, Mass Spectrometry, Membrane Proteins, Models, Molecular, Multiprotein Complexes, Protein Subunits