Dodecyl maltoside protects membrane proteins in vacuo.
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.
Department of Biochemistry, University of Oxford, United Kingdom.
Sarah L
SL
Rouse
Julien
J
Marcoux
Carol V
CV
Robinson
Mark S P
MS
Sansom
D000595:Amino Acid Sequence; D003681:Dehydration; D005960:Glucosides / Q000737:chemistry / Q000494:pharmacology*; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008823:Micelles; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D014618:Vacuum; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism
C064964:BM2 polypeptide, influenza B virus; D005960:Glucosides; D008565:Membrane Proteins; D008823:Micelles; D014764:Viral Proteins; C040358:dodecyl maltoside