[NMR paper] Molecular motions and interactions in aqueous solutions of thymosin-ß4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy.
Related ArticlesMolecular 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 aqueous solutions of thymosin-?4 (T?4), stabilin C-terminal domain (CTD) and their 1:1 complex. The energy distributions of the potential barriers, which control motion of protein-bound water molecules, were determined. Heterogeneous and homo-geneous regions were found in the protein-water interface. The measure of heterogeneity give quantitative value for the portion of disordered parts in the protein. Ordered structural elements were found extending up to 20% of the 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. According to the used terminology, 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: 29274195 [PubMed - as supplied by publisher]
Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function
Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function
Publication date: February 2016
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volumes 92–93</br>
Author(s): George P. Lisi, J. Patrick Loria</br>
Conformational motions play an essential role in enzyme function, often facilitating the formation of enzyme-substrate complexes and/or product release. Although considerable debate remains regarding the role of molecular motions in the conversion of enzymatic substrates to products, numerous examples have found motions...
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04-09-2016 03:54 AM
[NMR paper] Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations.
Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations.
Related Articles Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations.
Phys Chem Chem Phys. 2015 Oct 9;
Authors: Paluch P, Pawlak T, Jeziorna A, Trébosc J, Hou G, Vega AJ, Amoureux JP, Dracinsky M, Polenova T, Potrzebowski MJ
Abstract
We report a new multidimensional magic angle spinning...
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10-10-2015 06:47 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, 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...
Molecular motions and interactions in aqueous solutions of thymosin-ß4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy.
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