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
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
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
[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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03-03-2020 11:18 PM
Dynamic Nuclear Polarization/Solid-State NMR Spectroscopy of Membrane Polypeptides: Free-Radical Optimization for Matrix-Free Lipid Bilayer Samples #DNPNMR
From The DNP-NMR Blog:
Dynamic Nuclear Polarization/Solid-State NMR Spectroscopy of Membrane Polypeptides: Free-Radical Optimization for Matrix-Free Lipid Bilayer Samples #DNPNMR
p.p1 {margin: 0.0px 0.0px 0.0px 36.0px; text-indent: -36.0px; font: 12.0px Helvetica}
Salnikov, E.S., et al., Dynamic Nuclear Polarization/Solid-State NMR Spectroscopy of Membrane Polypeptides: Free-Radical Optimization for Matrix-Free Lipid Bilayer Samples. ChemPhysChem, 2017. 18(15): p. 2103-2113.
https://www.ncbi.nlm.nih.gov/pubmed/28574169
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09-25-2017 08:42 PM
[NMR paper] Dynamic nuclear polarization / solid-state NMR of membrane polypeptides. Free radical optimization for matrix-free lipid bilayer samples.
Dynamic nuclear polarization / solid-state NMR of membrane polypeptides. Free radical optimization for matrix-free lipid bilayer samples.
Related Articles Dynamic nuclear polarization / solid-state NMR of membrane polypeptides. Free radical optimization for matrix-free lipid bilayer samples.
Chemphyschem. 2017 Jun 02;:
Authors: Ouari O, Salnikov ES, Abel S, Karthikeyan G, Karoui H, Aussenac F, Tordo P, Bechinger B
Abstract
Dynamic Nuclear Polarization boosts the sensitivity of NMR spectroscopy by orders of magnitude making...
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06-03-2017 11:49 AM
Detergent-free Isolation of Functional G Protein-CoupledReceptors into Nanometric Lipid Particles
Detergent-free Isolation of Functional G Protein-CoupledReceptors into Nanometric Lipid Particles
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01040/20151223/images/medium/bi-2015-01040n_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01040
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/Mw6e22AdGJI
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12-28-2015 12:26 AM
[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...
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04-03-2014 12:59 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
[NMR paper] NMR study of a membrane protein in detergent-free aqueous solution.
NMR study of a membrane protein in detergent-free aqueous solution.
Related Articles NMR study of a membrane protein in detergent-free aqueous solution.
Proc Natl Acad Sci U S A. 2005 Jun 21;102(25):8893-8
Authors: Zoonens M, Catoire LJ, Giusti F, Popot JL
One of the major obstacles to membrane protein (MP) structural studies is the destabilizing effect of detergents. Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep MPs water-soluble under mild conditions. In the present work, we have explored the...