Nondestructive Investigation of the Agglomeration Process for Nanosuspensions via NMR Relaxation of Water Molecules

2021 ◽  
pp. 105908
Author(s):  
Kotaro Okada ◽  
Yoshihiro Hayashi ◽  
Shungo Kumada ◽  
Yoshinori Onuki
Keyword(s):  
Nmr Relaxation ◽  
Water Molecules ◽  
Agglomeration Process ◽  
Nondestructive Investigation

scholarly journals Water-Protein Interactions: The Secret of Protein Dynamics

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Silvia Martini ◽  
Claudia Bonechi ◽  
Alberto Foletti ◽  
Claudio Rossi
Keyword(s):  
Protein Interactions ◽  
Nmr Relaxation ◽  
Spin Lattice Relaxation ◽  
Resonance Spectroscopy ◽  
Water Molecules ◽  
Hydration Water ◽  
Relaxation Rates ◽  
Relaxation Parameters ◽  
Hydration Shells ◽  
Dynamical Properties

Water-protein interactions help to maintain flexible conformation conditions which are required for multifunctional protein recognition processes. The intimate relationship between the protein surface and hydration water can be analyzed by studying experimental water properties measured in protein systems in solution. In particular, proteins in solution modify the structure and the dynamics of the bulk water at the solute-solvent interface. The ordering effects of proteins on hydration water are extended for several angstroms. In this paper we propose a method for analyzing the dynamical properties of the water molecules present in the hydration shells of proteins. The approach is based on the analysis of the effects of protein-solvent interactions on water protons NMR relaxation parameters. NMR relaxation parameters, especially the nonselective (R1NS) and selective (R1SE) spin-lattice relaxation rates of water protons, are useful for investigating the solvent dynamics at the macromolecule-solvent interfaces as well as the perturbation effects caused by the water-macromolecule interactions on the solvent dynamical properties. In this paper we demonstrate that Nuclear Magnetic Resonance Spectroscopy can be used to determine the dynamical contributions of proteins to the water molecules belonging to their hydration shells.

Molecular Mobility of the Water Molecules in Aqueous Sucrose Solutions, Studied by 2H-NMR Relaxation

1994 ◽  
Vol 49 (3-4) ◽  
pp. 250-257 ◽  
Author(s):  
D. Girlich ◽  
H.-D. Lüdemann
Keyword(s):  
Temperature Dependence ◽  
Relaxation Times ◽  
Nmr Relaxation ◽  
Lattice Relaxation ◽  
Spin Lattice Relaxation ◽  
Water Molecules ◽  
Spin Lattice ◽  
Sucrose Solutions ◽  
Deuteron Spin ◽  
High Concentrations

Deuteron spin lattice relaxation times T1 of sucrose/D2O solutions are given as function of temperature, pressure, frequency and concentration. From the temperature dependence of the 2H -T1 the rotational dynamics of the hydrated sucrose complex and the water molecules are determined. For high pressure and high concentrations the temperature dependence of the water molecules is described by a Vogel-Tammann-Fulcher equation. The ideal glass transition temperatures TOH2O derived for the water molecules are at higher concentrations almost constant and smaller than the TOsuc of the sugar molecules

NMR relaxation study of water molecules in concentrated zinc chloride solutions

1982 ◽  
Vol 77 (6) ◽  
pp. 3258-3262 ◽  
Author(s):  
Yoshio Nakamura ◽  
Shigezo Shimokawa ◽  
Katsuya Futamata ◽  
Mitsuo Shimoji
Keyword(s):  
Zinc Chloride ◽  
Nmr Relaxation ◽  
Water Molecules ◽  
Chloride Solutions ◽  
Relaxation Study

NMR Relaxation Study of the Thermal Denaturation of Lysozyme

1975 ◽  
Vol 30 (3-4) ◽  
pp. 294-295 ◽  
Author(s):  
D. Pumpernik ◽  
B. Fajt ◽  
S. Lapanje ◽  
A. Ažman
Keyword(s):  
Thermal Denaturation ◽  
Relaxation Times ◽  
Nmr Relaxation ◽  
Methyl Groups ◽  
Water Molecules ◽  
Relaxation Study

Abstract Lysozyme relaxation times T1 and T2 have been measured. Methyl groups T1 are sensitive to thermal denaturation of the lysozyme. The exchange of the water molecules between bounded and free is slow

Strukturen zweier isomerer Gadolinium(III)-Polyaminopolycarboxylate -Argumente für signifikante Unterschiede ihrer 1H-NMR-Relaxation/Structures of Two Isomeric Gadolinium(III) Polyamino Polycarboxylates -Relation to their Significant Differences in 1H NMR Relaxation

1997 ◽  
Vol 52 (7) ◽  
pp. 805-809 ◽  
Author(s):  
Robert Ruloff ◽  
Thomas Gelbrich ◽  
Joachim Sieler ◽  
Eberhard Hoyer ◽  
Lothar Beyer
Keyword(s):  
Aqueous Solution ◽  
Crystal Structures ◽  
Coordination Number ◽  
1H Nmr ◽  
Nmr Relaxation ◽  
Acetate Group ◽  
Water Molecules ◽  
X Ray ◽  
H Nmr ◽  
Low Efficiency

Abstract We present preparation and X-ray crystal structures of gadolinium(III) complexes with two isomeric ligands; triethylenetetraminehexaacetic acid, H6ttha, and tris(2-aminoethyl)amine-hexaacetic acid, H6ttaha, respectively. In case of [C(NH2)3]2[Gd(Httha)] · 5 H2O (1) the inner coordination sphere is made up of 9 donor atoms of the ligand and reflects the low efficiency in accelerating 1H NMR relaxation of an aqueous solution. In case of [C(NH2)3]3[Gd(ttaha)] · 3 H2O (2) the coordination number of 9 is realized via 7 donor atoms of the ligand and 2 oxygen atoms of a pending acetate group of the adjacent complex. Luminescence studies in aqueous solution confirm replacement of this acetate group by 2 water molecules. The relaxivity of [Gd(Httaha)]2- is 7.3 ± 0.1 mM -1 s -1 as determined at pH = 7.2, 20 MHz and 40°C.

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