[NMR paper] Structural characterization of triple transmembrane domain containing fragments of a yeast G protein-coupled receptor in an organic : aqueous environment by solution-state NMR spectroscopy.
Structural characterization of triple transmembrane domain containing fragments of a yeast G protein-coupled receptor in an organic : aqueous environment by solution-state NMR spectroscopy.
Related ArticlesStructural characterization of triple transmembrane domain containing fragments of a yeast G protein-coupled receptor in an organic : aqueous environment by solution-state NMR spectroscopy.
J Pept Sci. 2015 Feb 2;
Authors: Fracchiolla KE, Cohen LS, Arshava B, Poms M, Zerbe O, Becker JM, Naider F
[NMR paper] Solution NMR studies reveal the location of the second transmembrane domain of the human sigma-1 receptor.
Solution NMR studies reveal the location of the second transmembrane domain of the human sigma-1 receptor.
Related Articles Solution NMR studies reveal the location of the second transmembrane domain of the human sigma-1 receptor.
FEBS Lett. 2015 Jan 31;
Authors: Ortega-Roldan JL, Ossa F, Amin NT, Schnell JR
Abstract
The sigma-1 receptor (S1R) is a ligand-regulated membrane chaperone protein associated with endoplasmic reticulum stress response, and modulation of ion channel activities at the plasma membrane. We report here...
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02-04-2015 09:57 PM
[NMR paper] Toll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: an NMR structural study.
Toll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: an NMR structural study.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Toll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: an NMR structural study.
FEBS Lett. 2014 Nov 3;588(21):3802-7
Authors: Mineev KS, Goncharuk SA, Arseniev AS
Abstract
Toll-like receptors (TLRs) take part in both the innate and...
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0
01-23-2015 03:23 PM
[NMR paper] The dynamics of the G protein-coupled neuropeptide Y2 receptor in monounsaturated membranes investigated by solid-state NMR spectroscopy.
The dynamics of the G protein-coupled neuropeptide Y2 receptor in monounsaturated membranes investigated by solid-state NMR spectroscopy.
The dynamics of the G protein-coupled neuropeptide Y2 receptor in monounsaturated membranes investigated by solid-state NMR spectroscopy.
J Biomol NMR. 2015 Jan 6;
Authors: Thomas L, Kahr J, Schmidt P, Krug U, Scheidt HA, Huster D
Abstract
In contrast to the static snapshots provided by protein crystallography, G protein-coupled receptors constitute a group of proteins with highly dynamic...
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01-06-2015 07:59 PM
The dynamics of the G protein-coupled neuropeptide Y2 receptor in monounsaturated membranes investigated by solid-state NMR spectroscopy
The dynamics of the G protein-coupled neuropeptide Y2 receptor in monounsaturated membranes investigated by solid-state NMR spectroscopy
Abstract
In contrast to the static snapshots provided by protein crystallography, G protein-coupled receptors constitute a group of proteins with highly dynamic properties, which are required in the receptorsâ?? function as signaling molecule. Here, the human neuropeptide Y2 receptor was reconstituted into a model membrane composed of monounsaturated phospholipids and solid-state NMR was used to characterize...
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Abstract Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties with achieving proper folding, membrane insertion, and native-like post-translational modifications frequently disqualify bacterial expression systems. On the other hand, eukaryotic cell cultures can be prohibitively expensive. One of the viable alternatives,...
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Proteins
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01-22-2011 03:46 AM
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
J Biomol NMR. 2011 Jan 19;
Authors: Fan Y, Shi L, Ladizhansky V, Brown LS
Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties...
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01-21-2011 01:22 AM
[NMR paper] Solution NMR spectroscopy of the human vasopressin V2 receptor, a G protein-coupled r
Solution NMR spectroscopy of the human vasopressin V2 receptor, a G protein-coupled receptor.
Related Articles Solution NMR spectroscopy of the human vasopressin V2 receptor, a G protein-coupled receptor.
J Am Chem Soc. 2005 Jun 8;127(22):8010-1
Authors: Tian C, Breyer RM, Kim HJ, Karra MD, Friedman DB, Karpay A, Sanders CR
The seven-transmembrane-spanning G protein-coupled receptor (GPCR) superfamily plays many important roles in basic biology, human health, and human disease. Here, well-resolved solution NMR spectra are presented for a human...
Structural characterization of triple transmembrane domain containing fragments of a yeast G protein-coupled receptor in an organic : aqueous environment by solution-state NMR spectroscopy.
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