Dodecyl maltoside protects membrane proteins in vacuo.

Journal article

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.

Authors: Rouse, S; Marcoux, J; Robinson, C; Sansom, MS

• Publication status: Published
• Peer review status: Peer reviewed
• Publisher: Elsevier
• Journal: Biophysical journal
• Volume: 105
• Issue: 3
• Pages: 648-656
• Publication date: 2013-08-01
• DOI: 10.1016/j.bpj.2013.06.025
• EISSN: 1542-0086
• ISSN: 0006-3495
• Language: English
• Keywords: Vacuum; Protein Structure, Tertiary; Viral Proteins; Protein Stability; Molecular Sequence Data; Dehydration; Glucosides; Molecular Dynamics Simulation; Membrane Proteins; Amino Acid Sequence; Micelles