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...
[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...
[NMR paper] NMR study of histidine metabolism during alcoholic and malolactic fermentations of wine and their influence on histamine production.
NMR study of histidine metabolism during alcoholic and malolactic fermentations of wine and their influence on histamine production.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles NMR study of histidine metabolism during alcoholic and malolactic fermentations of wine and their influence on histamine production.
J Agric Food Chem. 2013 Oct 2;61(39):9464-9
Authors: López-Rituerto E, Avenoza A, Busto JH, Peregrina JM
Abstract
The metabolic pathways...
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07-16-2014 10:46 AM
[NMR paper] Effects of a type I antifreeze protein (AFP) on the melting of frozen AFP and AFP+solute aqueous solutions studied by NMR microimaging experiment.
Effects of a type I antifreeze protein (AFP) on the melting of frozen AFP and AFP+solute aqueous solutions studied by NMR microimaging experiment.
Related Articles Effects of a type I antifreeze protein (AFP) on the melting of frozen AFP and AFP+solute aqueous solutions studied by NMR microimaging experiment.
J Biol Phys. 2013 Jan;39(1):131-44
Authors: Ba Y, Mao Y, Galdino L, Günsen Z
Abstract
The effects of a type I AFP on the bulk melting of frozen AFP solutions and frozen AFP+solute solutions were studied through an NMR...
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07-19-2013 09:20 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, WĂźthrich 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...
Production of a Human Histamine Receptor for NMR Spectroscopy in Aqueous Solutions
Linear Mode
