ArticleEuropean biophysics journal : EBJ2011
Membrane protein dynamics in different environments: simulation study of the outer membrane protein X in a lipid bilayer and in a micelle.
Article in European biophysics journal : EBJ, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- How Do Short Chain Nonionic Detergents Destabilize G-Protein-Coupled Receptors?Journal of the American Chemical Society · 2016Article
- Virulence characteristics of extraintestinal pathogenic Escherichia coli deletion of gene encoding the outer membrane protein X.The Journal of veterinary medical science · 2016Article
- Interactions of lipids and detergents with a viral ion channel protein: molecular dynamics simulation studies.The journal of physical chemistry. B · 2015Article
- Molecular dynamics simulations of a membrane protein/amphipol complex.The Journal of membrane biology · 2014Article
- Detergent-mediated protein aggregation.Chemistry and physics of lipids · 2013Review
- Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins.Journal of the American Chemical Society · 2013Article
- On the role of NMR spectroscopy for characterization of antimicrobial peptides.Methods in molecular biology (Clifton, N.J.) · 2013Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial outer membrane protein OmpX from Escherichia coli has been investigated by molecular dynamics simulations when embedded in a phospholipid bilayer and as a protein-micelle aggregate. The resulting simulation trajectories were analysed in terms of structural and dynamic properties of the membrane protein. In agreement with experimental observations, highest relative stability was found for the β-barrel region that is embedded in the lipophilic phase, whereas an extracellular protruding β-sheet, which is a unique structural feature of OmpX that supposedly plays an important role in cell adhesion and invasion, shows larger structure fluctuations. Additionally, we investigated water permeation into the core of the β-barrel protein, which contains a tight salt-bridge and hydrogen-bond network, so that extensive water flux is unlikely. Differences between the bilayer and the micellar system were observed in the length of the barrel and its position inside the lipid environment, and in the protein interactions with the hydrophilic part of the lipids near the lipid/water interface. Those variations suggest that micelles and other detergent environments might not offer a wholly membrane-like milieu to promote adoption of the physiological conformational state by OmpX.
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Registered trials
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