ArticleProtein science : a publication of the Protein Society2014
Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 36 citations in OpenAlex.
- Polymer-Nanodiscs as a Novel Alignment Medium for High-Resolution NMR-Based Structural Studies of Nucleic Acids.Biomolecules · 2022Article
- Saponins Form Nonionic Lipid Nanodiscs for Protein Structural Studies by Nuclear Magnetic Resonance Spectroscopy.The journal of physical chemistry letters · 2022Article
- Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR.Biology · 2020Review
- Solution NMR: A powerful tool for structural and functional studies of membrane proteins in reconstituted environments.The Journal of biological chemistry · 2019Review
- 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
- A Minimal Functional Complex of Cytochrome P450 and FBD of Cytochrome P450 Reductase in Nanodiscs.Angewandte Chemie (International ed. in English) · 2018Article
- Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR.Nature protocols · 2018Article
- Lipid Internal Dynamics Probed in Nanodiscs.Chemphyschem : a European journal of chemical physics and physical chemistry · 2017Article
- Application of Solution NMR to Structural Studies on α-Helical Integral Membrane Proteins.Molecules (Basel, Switzerland) · 2017Review
- Review
- Nanodiscs and Solution NMR: preparation, application and challenges.Nanotechnology reviews · 2017Article
- Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I.Nature structural & molecular biology · 2017Article
- Micelles, Bicelles, and Nanodiscs: Comparing the Impact of Membrane Mimetics on Membrane Protein Backbone Dynamics.Angewandte Chemie (International ed. in English) · 2017Article
- Structure refinement and membrane positioning of selectively labeled OmpX in phospholipid nanodiscs.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
- Influence of the lipid membrane environment on structure and activity of the outer membrane protein Ail from Yersinia pestis.Biochimica et biophysica acta · 2015Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane proteins are involved in numerous vital biological processes. To understand membrane protein functionality, accurate structural information is required. Usually, structure determination and dynamics of membrane proteins are studied in micelles using either solution state NMR or X-ray crystallography. Even though invaluable information has been obtained by this approach, micelles are known to be far from ideal mimics of biological membranes often causing the loss or decrease of membrane protein activity. Recently, nanodiscs, which are composed of a lipid bilayer surrounded by apolipoproteins, have been introduced as a more physiological alternative than micelles for NMR investigations on membrane proteins. Here, we show that membrane protein bond orientations in nanodiscs can be obtained by measuring residual dipolar couplings (RDCs) with the outer membrane protein OmpX embedded in nanodiscs using Pf1 phage as an alignment medium. The presented collection of membrane protein RDCs in nanodiscs represents an important step toward more comprehensive structural and dynamical NMR-based investigations of membrane proteins in a natural bilayer environment.
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