Related ArticlesRelaxation-matrix formalism for rotating-frame spin-lattice proton NMR relaxation and magnetization transfer in the presence of an off-resonance irradiation field.
J Magn Reson B. 1994 May;104(1):11-25
Authors: Kuwata K, Brooks D, Yang H, Schleich T
The derivation of a generalized relaxation matrix equation for the off-resonance rotating-frame spin-lattice experiment, representing N macromolecular components, is presented. The applicability of the derived formalism was demonstrated using water proton off-resonance rotating-frame spin-lattice relaxation data obtained for calf lens cortical and nuclear homogenates, a tissue system characterized by the presence of both mobile and solid-like protein domains, whose relative amounts vary in a protein-concentration-dependent manner. Protein concentration and temperature were utilized as variables in the magnetization-transfer experiments. Curve fitting to obtain the relevant magnetization-transfer parameters was accomplished by simulated annealing and the method of steepest descents. In all cases, the best fit, as reflected by the smallest root-mean-square deviation, was obtained by assuming the presence of three components representing bulk-water and mobile and solid-like macromolecular components, characterized by Lorentzian (water and mobile protein) and Gaussian proton resonance lineshapes (solid-like protein). A two-component relaxation model gave unsatisfactory fits. Dilution of nuclear homogenate resulted in physically realistic changes in the derived magnetization-transfer parameters, which included a decrease in the fraction of solid-like protein, in agreement with previously published 13C NMR studies. Changes in magnetization-transfer parameters occurred as a result of the cold cataract phase transition in nuclear homogenate. The utility and limitations of the derived formalism are discussed.
Water proton spin saturation affects measured protein backboneN spin relaxation rates
Water proton spin saturation affects measured protein backboneN spin relaxation rates
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 1 October 2011</br>
Kang*Chen, Nico*Tjandra</br>
Protein backboneN NMR spin relaxation rates are useful in characterizing the protein dynamics and structures. To observe the protein nuclear-spin resonances a pulse sequence has to include a water suppression scheme. There are two commonly employed methods, saturating or dephasing the water spins with pulse field gradients and keeping them unperturbed with flip-back pulses....
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[NMR paper] An NMR study of the origin of dioxygen-induced spin-lattice relaxation enhancement an
An NMR study of the origin of dioxygen-induced spin-lattice relaxation enhancement and chemical shift perturbation.
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J Magn Reson. 2004 Dec;171(2):225-32
Authors: Prosser RS, Luchette PA
Due to its depth-dependent solubility, oxygen exerts paramagnetic effects which become progressively greater toward the hydrophobic interior of micelles, and lipid bilayer membranes. This paramagnetic gradient, which is manifested...
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Water-Proton-Spin-Lattice-Relaxation Dispersion of Paramagnetic Protein Solutions
Water-Proton-Spin-Lattice-Relaxation Dispersion of Paramagnetic Protein Solutions
Publication year: 2010
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 10 November 2010</br>
Galina, Diakova , Yanina, Goddard , Jean-Pierre, Korb , Robert G., Bryant</br>
The paramagnetic contributions to water proton spin-lattice relaxation rate constants in protein systems spin-labeled with nitroxide radicals were re-examined. As noted by others, the strength of the dipolar coupling between water protons and the protein-bound nitroxide radical often appears to...
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Hydration water dynamics in biopolymers from NMR relaxation in the rotating frame.
Hydration water dynamics in biopolymers from NMR relaxation in the rotating frame.
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J Magn Reson. 2010 Sep 24;
Authors: Blicharska B, Peemoeller H, Witek M
Assuming dipole-dipole interaction as the dominant relaxation mechanism of protons of water molecules adsorbed onto macromolecule (biopolymer) surfaces we have been able to model the dependences of relaxation rates on temperature and frequency. For adsorbed water molecules the correlation times are...
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[NMR paper] Relaxation-matrix formalism for rotating-frame spin-lattice proton NMR relaxation and
Relaxation-matrix formalism for rotating-frame spin-lattice proton NMR relaxation and magnetization transfer in the presence of an off-resonance irradiation field.
Related Articles Relaxation-matrix formalism for rotating-frame spin-lattice proton NMR relaxation and magnetization transfer in the presence of an off-resonance irradiation field.
J Magn Reson B. 1994 May;104(1):11-25
Authors: Kuwata K, Brooks D, Yang H, Schleich T
The derivation of a generalized relaxation matrix equation for the off-resonance rotating-frame spin-lattice...
nmrlearner
Journal club
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08-22-2010 03:33 AM
[NMR paper] A 31P-NMR spin-lattice relaxation and 31P[1H] nuclear Overhauser effect study of soni
A 31P-NMR spin-lattice relaxation and 31P nuclear Overhauser effect study of sonicated small unilamellar phosphatidylcholine vesicles.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A 31P-NMR spin-lattice relaxation and 31P nuclear Overhauser effect study of sonicated small unilamellar phosphatidylcholine vesicles.
Biochim Biophys Acta. 1992 Feb 17;1104(1):137-46
Authors: Tauskela JS, Thompson M
The motional properties of the inner and outer monolayer headgroups of...
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[NMR paper] Off-resonance rotating frame spin-lattice NMR relaxation studies of phosphorus metabo
Off-resonance rotating frame spin-lattice NMR relaxation studies of phosphorus metabolite rotational diffusion in bovine lens homogenates.
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Biochemistry. 1990 Aug 21;29(33):7547-57
Authors: Caines GH, Schleich T, Morgan CF, Farnsworth PN
The rotational diffusion behavior of phosphorus metabolites present in calf lens cortical and nuclear homogenates was investigated by the NMR technique of...
Relaxation-matrix formalism for rotating-frame spin-lattice proton NMR relaxation and
Linear Mode
