[NMR paper] Molecular motions and interactions in aqueous solutions of thymosin-?4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy.
Related ArticlesMolecular 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 aqueous solutions of thymosin-? 4 (T? 4 ), stabilin C-terminal domain (CTD) and their 1:1 complex. Energy distributions of potential barriers controlling the motion of protein-bound water molecules were determined. Heterogeneous and homogeneous regions were found in the protein-water interface. The measure of heterogeneity of this interface gives quantitative value for the portion of disordered parts in the protein. Ordered structural elements were found extending up to ~20% of the individual whole proteins. About 40% of the binding sites of free T? 4 get involved in bonds holding the complex together. The complex has the most heterogeneous solvent accessible surface (SAS) in terms of protein-water interactions. The complex is more disordered than T? 4 or stabilin CTD. The greater SAS area of the complex is interpreted as a clear sign of its open structure.
PMID: 32469123 [PubMed - as supplied by publisher]
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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[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
[NMR paper] Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.
Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.
Related Articles Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.
J Biol Chem. 2014 Aug 13;
Authors: Meneses E, Mittermaier A
Abstract
Much of our knowledge of protein binding pathways is derived from extremely stable complexes that interact very tightly, with lifetimes of hours to days. Much less is known about...
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08-15-2014 12:53 PM
[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] Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
J Am Chem Soc. 2013 Apr 29;
Authors: Scanu S, Förster J, Ullmann GM, Ubbink M
Abstract
Protein complex formation is thought to be at least a two-step process, in which the active complex is preceded by the formation of an encounter complex....
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05-01-2013 11:46 AM
[NMR paper] Protein-Carbohydrate Interactions Studied by NMR. from Molecular Recognition to Drug Design.
Protein-Carbohydrate Interactions Studied by NMR. from Molecular Recognition to Drug Design.
Related Articles Protein-Carbohydrate Interactions Studied by NMR. from Molecular Recognition to Drug Design.
Curr Protein Pept Sci. 2012 Dec 10;
Authors: Fernandez-Alonso MD, Diaz D, Berbis MA, Marcelo F, Jimenez-Barbero J
Abstract
Diseases that result from infection are, in general, a consequence of specific interactions between a pathogenic organism and the cells. The study of host-pathogen interactions has provided insights for the design of...
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02-03-2013 10:22 AM
[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...
Molecular motions and interactions in aqueous solutions of thymosin-?4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy.
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