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...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
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Elsevier
2013
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| _version_ | 1826264994181808128 |
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| author | Rouse, S Marcoux, J Robinson, C Sansom, MS |
| author_facet | Rouse, S Marcoux, J Robinson, C Sansom, MS |
| author_sort | Rouse, S |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T20:16:42Z |
| format | Journal article |
| id | oxford-uuid:2c5e8a95-0403-474b-8795-7ae2d63c8aa8 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T20:16:42Z |
| publishDate | 2013 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | oxford-uuid:2c5e8a95-0403-474b-8795-7ae2d63c8aa82022-03-26T12:36:40ZDodecyl maltoside protects membrane proteins in vacuo.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:2c5e8a95-0403-474b-8795-7ae2d63c8aa8EnglishSymplectic Elements at OxfordElsevier2013Rouse, SMarcoux, JRobinson, CSansom, MSMolecular 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. |
| spellingShingle | Rouse, S Marcoux, J Robinson, C Sansom, MS Dodecyl maltoside protects membrane proteins in vacuo. |
| title | Dodecyl maltoside protects membrane proteins in vacuo. |
| title_full | Dodecyl maltoside protects membrane proteins in vacuo. |
| title_fullStr | Dodecyl maltoside protects membrane proteins in vacuo. |
| title_full_unstemmed | Dodecyl maltoside protects membrane proteins in vacuo. |
| title_short | Dodecyl maltoside protects membrane proteins in vacuo. |
| title_sort | dodecyl maltoside protects membrane proteins in vacuo |
| work_keys_str_mv | AT rouses dodecylmaltosideprotectsmembraneproteinsinvacuo AT marcouxj dodecylmaltosideprotectsmembraneproteinsinvacuo AT robinsonc dodecylmaltosideprotectsmembraneproteinsinvacuo AT sansomms dodecylmaltosideprotectsmembraneproteinsinvacuo |