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Dodecyl maltoside protects membrane proteins in vacuo.

ABSTRACT: 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 ?-helical bundle versus a ?-barrel) and two different detergent types (phosphocholines versus an alkyl sugar) with respect to protein stability and detergent packing. The ?-barrel membrane protein remained stable as a protein-detergent complex in vacuum. Zwitterionic detergents formed conformationally destabilizing interactions with an ?-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.

SUBMITTER: Rouse SL

PROVIDER: S-EPMC3736684 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature

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Dodecyl maltoside protects membrane proteins in vacuo.

Rouse Sarah L SL Marcoux Julien J Robinson Carol V CV Sansom Mark S P MS

Biophysical journal 20130801 3

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 com ...[more]

PMID: 23931313

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