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Molecular dynamics simulations have been used to characterize the effects of transfer from aqueous solution to a vacuum to inform our understanding of mass spectrometry of membrane-protein-detergent complexes. We compared two membrane protein architectures (an α-helical bundle versus a β-barrel) and two different detergent types (phosphocholines versus an alkyl sugar) with respect to protein stability and detergent packing. The β-barrel membrane protein remained stable as a protein-detergent complex in vacuum. Zwitterionic detergents formed conformationally destabilizing interactions with an α-helical membrane protein after detergent micelle inversion driven by dehydration in vacuum. In contrast, a nonionic alkyl sugar detergent resisted micelle inversion, maintaining the solution-phase conformation of the protein. This helps to explain the relative stability of membrane proteins in the presence of alkyl sugar detergents such as dodecyl maltoside.

Original publication

DOI

10.1016/j.bpj.2013.06.025

Type

Journal article

Journal

Biophys J

Publication Date

06/08/2013

Volume

105

Pages

648 - 656

Keywords

Amino Acid Sequence, Dehydration, Glucosides, Membrane Proteins, Micelles, Molecular Dynamics Simulation, Molecular Sequence Data, Protein Stability, Protein Structure, Tertiary, Vacuum, Viral Proteins