ArticleChembiochem : a European journal of chemical biology2014
Solution-NMR characterization of outer-membrane protein A from E. coli in lipid bilayer nanodiscs and detergent micelles.
Article in Chembiochem : a European journal of chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Solution NMR Spectroscopy for the Determination of Structures of Membrane Proteins in a Lipid Environment.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- Sparse pseudocontact shift NMR data obtained from a non-canonical amino acid-linked lanthanide tag improves integral membrane protein structure prediction.Journal of biomolecular NMR · 2023Article
- A comparative study of interfacial environments in lipid nanodiscs and vesicles.Biophysical reports · 2022Article
- Kinetic analysis of antibody binding to integral membrane proteins stabilized in SMALPs.BBA advances · 2021Article
- Folding of the β-Barrel Membrane Protein OmpA into Nanodiscs.Biophysical journal · 2020Article
- The hydrodynamic motion of Nanodiscs.Chemistry and physics of lipids · 2019Article
- Elucidating the Lipid Binding Properties of Membrane-Active Peptides Using Cyclised Nanodiscs.Frontiers in chemistry · 2019Article
- Measuring translational diffusion ofEuropean biophysics journal : EBJ · 2018Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR.Nature protocols · 2018Article
- Structural Insights into the Yersinia pestis Outer Membrane Protein Ail in Lipid Bilayers.The journal of physical chemistry. B · 2017Article
- Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017Review
- Review
- Nanodiscs and Solution NMR: preparation, application and challenges.Nanotechnology reviews · 2017Article
- Combining Mass Spectrometry and X-Ray Crystallography for Analyzing Native-Like Membrane Protein Lipid Complexes.Frontiers in physiology · 2017Article
- Full-Length OmpA: Structure, Function, and Membrane Interactions Predicted by Molecular Dynamics Simulations.Biophysical journal · 2016Article
- Micro-scale NMR Experiments for Monitoring the Optimization of Membrane Protein Solutions for Structural Biology.Bio-protocol · 2015Article
- Optimizing nanodiscs and bicelles for solution NMR studies of two β-barrel membrane proteins.Journal of biomolecular NMR · 2015Article
- Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation.Journal of biomolecular NMR · 2015Article
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3 authors.
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Abstract
X-ray crystallography and solution NMR of detergent-reconstituted OmpA (outer membrane protein A from E. coli) had shown that this protein forms an eight-stranded transmembrane β-barrel, but only limited information was obtained for the extracellular loops. In NMR studies of OmpA in two different detergent micelles, "NMR-invisible" amino acid residues in-between the extracellular loops and the β-barrel prevented complete structural characterization. Here, we show that this NMR-invisible ring around the β-barrel of OmpA is also present in lipid bilayer nanodiscs and in mixed micelles with a third detergent, thus suggesting that the implicated rate processes have a functional role rather than representing an artifact of the protein reconstitution. In addition to sequence-specific NMR assignments for OmpA in the nanodiscs, the present results are based on a protocol of micro-coil TROSY- and CRINEPT-type NMR diffusion measurements for studying the hydrodynamic properties and the foldedness of [(2)H,(15)N]-labeled membrane proteins in nanodiscs. This protocol can be applied under conditions closely similar to those used for NMR structure determinations or crystallization trials.
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