Endogenous phospholipids influence the conformational equilibria of G protein-coupled receptors, regulating their ability to bind drugs and form signaling complexes. However, most studies of GPCR-lipid interactions have been carried out in mixed micelles or lipid nanodiscs. Though useful, these membrane mimetics do not fully replicate the physical properties of native cellular membranes associated with large assemblies of lipids. We investigated the conformational equilibria of the human A (2A)...
[NMR paper] Production of a Human Histamine Receptor for NMR Spectroscopy in Aqueous Solutions
Production of a Human Histamine Receptor for NMR Spectroscopy in Aqueous Solutions
G protein-coupled receptors (GPCRs) bind a broad array of extracellular molecules and transmit intracellular signals that initiate physiological responses. The signal transduction functions of GPCRs are inherently related to their structural plasticity, which can be experimentally observed by spectroscopic techniques. Nuclear magnetic resonance (NMR) spectroscopy in particular is an especially advantageous method to study the dynamic behavior of GPCRs. The success of NMR studies critically...
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04-30-2021 10:13 PM
[NMR paper] GPCR Activation States Induced by Nanobodies and Mini-G Proteins Compared by NMR Spectroscopy.
GPCR Activation States Induced by Nanobodies and Mini-G Proteins Compared by NMR Spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.png Related Articles GPCR Activation States Induced by Nanobodies and Mini-G Proteins Compared by NMR Spectroscopy.
Molecules. 2020 Dec 17;25(24):
Authors: Rößler P, Mayer D, Tsai CJ, Veprintsev DB, Schertler GFX, Gossert AD
Abstract
In this work, we examine methyl nuclear magnetic resonance (NMR) spectra of the...
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12-29-2020 04:50 AM
[NMR paper] Molecular motions and interactions in aqueous solutions of thymosin-?4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy.
Molecular motions and interactions in aqueous solutions of thymosin-?4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy.
Related Articles Molecular motions and interactions in aqueous solutions of thymosin-?4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy.
Chemphyschem. 2020 May 29;:
Authors: Bokor M, Tantos Á, Mészáros A, Jenei B, Haminda R, Tompa P, Tompa K
Abstract
Wide-line 1 H NMR measurements were extended and all results were interpreted in a thermodynamics* based new approach on...
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05-31-2020 03:53 PM
Concentration-dependent changes to diffusion and chemical shift of internal standard molecules in aqueous and micellar solutions
Concentration-dependent changes to diffusion and chemical shift of internal standard molecules in aqueous and micellar solutions
Abstract
Sodium 4,4-dimethyl-4-silapentane-1-sulfonate (DSS) is the most widely accepted internal standard for protein NMR studies in aqueous conditions. Since its introduction as a reference standard, however, concerns have been raised surrounding its propensity to interact with biological molecules through electrostatic and hydrophobic interactions. While DSS has been shown to interact with certain proteins, membrane...
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06-06-2018 01:42 PM
[NMR paper] Molecular motions and interactions in aqueous solutions of thymosin-ß4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy.
Molecular motions and interactions in aqueous solutions of thymosin-ß4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy.
Related Articles Molecular motions and interactions in aqueous solutions of thymosin-ß4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy.
Chemphyschem. 2017 Dec 23;:
Authors: Bokor M, Tantos Á, Mészáros A, Jenei B, Haminda R, Tompa P, Tompa K
Abstract
Wide-line 1H NMR measurements were extended and all results were reinterpreted in a thermodynamics based new approach on...
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12-24-2017 06:30 PM
Topologically Diverse Human Membrane Proteins Partitionto Liquid-Disordered Domains in Phase-Separated Lipid Vesicles
Topologically Diverse Human Membrane Proteins Partitionto Liquid-Disordered Domains in Phase-Separated Lipid Vesicles
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01154/20160210/images/medium/bi-2015-01154x_0003.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01154
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/FqvhNKDI0Xk
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02-11-2016 10:30 PM
TEMPOL as a polarizing agent for dynamic nuclear polarization of aqueous solutions
From The DNP-NMR Blog:
TEMPOL as a polarizing agent for dynamic nuclear polarization of aqueous solutions
Gafurov, M., TEMPOL as a polarizing agent for dynamic nuclear polarization of aqueous solutions. Magn. Reson. Solids., 2013. 15: p. 13103.
http://mrsej.ksu.ru/contents.html#13103
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05-03-2013 02:26 PM
[NMR paper] NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins.
NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins.
Related Articles NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins.
J Biomol NMR. 1992 Sep;2(5):447-65
Authors: Liepinsh E, Otting G, Wüthrich K
Hydroxyl groups of serine and threonine, and to some extent also tyrosine are usually located on or near the surface of proteins. NMR observations of the hydroxyl protons is therefore of interest to support investigations of the protein surface in solution, and knowledge of the...
The conformational equilibria of a human GPCR compared between lipid vesicles and aqueous solutions by integrative (19F) -NMR
Linear Mode
