ArticleBiochimica et biophysica acta2010
Fast-time scale dynamics of outer membrane protein A by extended model-free analysis of NMR relaxation data.
Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 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
- Opportunities and Challenges of Backbone, Sidechain, and RDC Experiments to Study Membrane Protein Dynamics in a Detergent-Free Lipid Environment Using Solution State NMR.Frontiers in molecular biosciences · 2019Review
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Solution NMR of SNAREs, complexin and α-synuclein in association with membrane-mimetics.Progress in nuclear magnetic resonance spectroscopy · 2018Review
- Expression, Functional Characterization, and Solid-State NMR Investigation of the G Protein-Coupled GHS Receptor in Bilayer Membranes.Scientific reports · 2017Article
- Unraveling the stereochemical and dynamic aspects of the catalytic site of bacterial peptidyl-tRNA hydrolase.RNA (New York, N.Y.) · 2017Article
- Micelles, Bicelles, and Nanodiscs: Comparing the Impact of Membrane Mimetics on Membrane Protein Backbone Dynamics.Angewandte Chemie (International ed. in English) · 2017Article
- NMR as a tool to investigate the structure, dynamics and function of membrane proteins.Nature structural & molecular biology · 2016Article
- The dynamics of the G protein-coupled neuropeptide Y2 receptor in monounsaturated membranes investigated by solid-state NMR spectroscopy.Journal of biomolecular NMR · 2015Article
- Ebolavirus entry requires a compact hydrophobic fist at the tip of the fusion loop.Journal of virology · 2014Article
- NMR-based conformational ensembles explain pH-gated opening and closing of OmpG channel.Journal of the American Chemical Society · 2013Article
- Membrane depth-dependent energetic contribution of the tryptophan side chain to the stability of integral membrane proteins.Biochemistry · 2013Article
- Lipid and membrane mimetic environments modulate spin label side chain configuration in the outer membrane protein A.The journal of physical chemistry. B · 2011Article
- Structural basis for the interaction of lipopolysaccharide with outer membrane protein H (OprH) from Pseudomonas aeruginosa.The Journal of biological chemistry · 2011Article
- Influence of solubilizing environments on membrane protein structures.Trends in biochemical sciences · 2011Review
- Functional dynamics in the voltage-dependent anion channel.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Solution structure and phospholipid interactions of the isolated voltage-sensor domain from KvAP.Journal of molecular biology · 2010Article
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3 authors.
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Abstract
In order to better understand the dynamics of an integral membrane protein, backbone amide (15)N NMR dynamics measurements of the beta-barrel membrane protein OmpA have been performed at three magnetic fields. A total of nine relaxation data sets were globally analyzed using an extended model-free formalism. The diffusion tensor was found to be prolate axially symmetric with an axial ratio of 5.75, indicating a possible rotation of the protein within the micelle. The generalized order parameters gradually decreased from the mid-plane towards the two ends of the barrel, counteracting the dynamic gradient of the lipids in a matching bilayer, and were dramatically reduced in the extracellular loops. Large-scale internal motions on the ns time scale indicate that entire loops most likely undergo concerted ("sea anemone"-like) motions emanating from their anchoring points on the barrel. The case of OmpA in DPC micelles also illustrates inherent limitations of analyzing the data with even the most sophisticated current models of the model-free formalism. It is likely that conformational exchange processes on the ms-mus also play a role in describing the motions of some residues, but their analysis did not produce unique results that could be independently verified.
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