ArticleThe Journal of membrane biology2014
Outer membrane protein F stabilised with minimal amphipol forms linear arrays and LPS-dependent 2D crystals.
Article in The Journal of membrane biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Complex Structural Examination of Protein-Lipid Interactions with Neutron Scattering Techniques.Methods in molecular biology (Clifton, N.J.) · 2026Review
- Exploiting neutron scattering contrast variation in biological membrane studies.Biophysics reviews · 2022Review
- A Surfactant Enables Efficient Membrane Spanning by Non-Aggregating DNA-Based Ion Channels.Molecules (Basel, Switzerland) · 2022Article
- Article
- Localized incorporation of outer membrane components in the pathogenThe EMBO journal · 2019Article
- Determining the amphipol distribution within membrane-protein fibre samples using small-angle neutron scattering.Acta crystallographica. Section D, Structural biology · 2018Article
- Article
- Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Amphipol-trapped ExbB-ExbD membrane protein complex from Escherichia coli: a biochemical and structural case study.The Journal of membrane biology · 2014Article
- The use of amphipols for NMR structural characterization of 7-TM proteins.The Journal of membrane biology · 2014Article
- High-resolution structure of a membrane protein transferred from amphipol to a lipidic mesophase.The Journal of membrane biology · 2014Article
- Amphipols for each season.The Journal of membrane biology · 2014Review
- Solution behavior and crystallization of cytochrome bc₁ in the presence of amphipols.The Journal of membrane biology · 2014Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Amphipols (APol) are polymers which can solubilise and stabilise membrane proteins (MP) in aqueous solutions. In contrast to conventional detergents, APol are able to keep MP soluble even when the free APol concentration is very low. Outer membrane protein F (OmpF) is the most abundant MP commonly found in the outer membrane (OM) of Escherichia coli. It plays a vital role in the transport of hydrophilic nutrients, as well as antibiotics, across the OM. In the present study, APol was used to solubilise OmpF to characterize its interactions with molecules such as lipopolysaccharides (LPS) or colicins. OmpF was reconstituted into APol by the removal of detergents using Bio-Beads followed by size-exclusion chromatography (SEC) to remove excess APol. OmpF/APol complexes were then analysed by SEC, dynamic light scattering (DLS) and transmission electron microscopy (TEM). TEM showed that in the absence of free APol-OmpF associated as long filaments with a thickness of ~6 nm. This indicates that the OmpF trimers lie on their sides on the carbon EM grid and that they also favour side by side association. The formation of filaments requires APol and occurs very rapidly. Addition of LPS to OmpF/APol complexes impeded filament formation and the trimers form 2D sheets which mimic the OM. Consequently, free APol is undoubtedly required to maintain the homogeneity of OmpF in solutions, but 'minimum APol' provides a new phase, which can allow weaker protein-protein and protein-lipid interactions characteristic of native membranes to take place and thus control 1D-2D crystallisation.
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