A quantitative assay to study the lipid selectivity of membrane-associated systems using solution NMR.
Chem Commun (Camb). 2020 Oct 07;56(78):11665-11668
Authors: Medina-Carmona E, Varela L, Hendry AC, Thompson GS, White LJ, Boles JE, Hiscock JR, Ortega-Roldan JL
Abstract
The activity of membrane proteins and compounds that interact with the membrane is modulated by the surrounding lipid composition. However, there are no simple methods that determine the composition of these annular phospholipids in eukaryotic systems. Herein, we describe a simple methodology that enables the identification and quantification of the lipid composition around membrane-associated compounds using SMA-nanodiscs and routine 1H-31P NMR.
[NMR paper] Exploring Lipid and Membrane Protein Dynamics Using Lipid-Bilayer Nanodiscs and Solution-State NMR Spectroscopy.
Exploring Lipid and Membrane Protein Dynamics Using Lipid-Bilayer Nanodiscs and Solution-State NMR Spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Exploring Lipid and Membrane Protein Dynamics Using Lipid-Bilayer Nanodiscs and Solution-State NMR Spectroscopy.
Methods Mol Biol. 2020;2127:397-419
Authors: Bibow S
Abstract
The relationship of membrane protein function and the surrounding lipid bilayer goes far beyond...
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[NMR paper] Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
PLoS One. 2017;12(9):e0184487
Authors: Delius J, Frank O, Hofmann T
Abstract
Nuclear magnetic resonance (NMR) spectroscopy is well-established in assessing the binding affinity between...
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[NMR paper] Solution-NMR Characterization of Outer-Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles.
Solution-NMR Characterization of Outer-Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles.
Related Articles Solution-NMR Characterization of Outer-Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles.
Chembiochem. 2014 Apr 1;
Authors: Sušac L, Horst R, Wüthrich K
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 ?-barrel, but only...
[NMR paper] A single-cell NMR membrane transport assay.
A single-cell NMR membrane transport assay.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles A single-cell NMR membrane transport assay.
Chembiochem. 2012 Nov 26;13(17):2501-4
Authors: Kremer W, Kalbitzer HR, Schreier C, Huber F, Schulze C, Daniel H, Stolz J
PMID: 23097137
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04-17-2013 08:15 PM
[NMR paper] Solution NMR spectroscopy for the determination of structures of membrane proteins in a lipid environment.
Solution NMR spectroscopy for the determination of structures of membrane proteins in a lipid environment.
Solution NMR spectroscopy for the determination of structures of membrane proteins in a lipid environment.
Methods Mol Biol. 2013;974:389-413
Authors: Arora A
Abstract
Several recent advancements have transformed solution NMR spectroscopy into a competitive, elegant, and eminently viable technique for determining the solution structures of membrane proteins at the level of atomic resolution. Once a good level of cell-based or...
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02-14-2013 02:37 PM
Solution NMR study of integral membrane proteins.
Solution NMR study of integral membrane proteins.
Solution NMR study of integral membrane proteins.
Curr Opin Chem Biol. 2011 Jun 18;
Authors: Kang C, Li Q
Signals between a cell and its environment are often transmitted through membrane proteins; therefore, many membrane proteins, including G protein-coupled receptors (GPCRs) and ion channels, are important drug targets. Structural information about membrane proteins remains limited owing to challenges in protein expression, purification and the selection of membrane-mimicking systems that will...
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[NMR paper] Lipid-protein stoichiometries in a crystalline biological membrane: NMR quantitative
Lipid-protein stoichiometries in a crystalline biological membrane: NMR quantitative analysis of the lipid extract of the purple membrane.
Related Articles Lipid-protein stoichiometries in a crystalline biological membrane: NMR quantitative analysis of the lipid extract of the purple membrane.
J Lipid Res. 2002 Jan;43(1):132-40
Authors: Corcelli A, Lattanzio VM, Mascolo G, Papadia P, Fanizzi F
The lipid/protein stoichiometries of a naturally crystalline biological membrane, the purple membrane (PM) of Halobacterium salinarum, have been...