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Relevant bibliographies by topics / Relaxation processes in nuclear magnetic resonance molecules

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Academic literature on the topic 'Relaxation processes in nuclear magnetic resonance molecules'

Author: Grafiati

Published: 17 September 2021

Last updated: 1 February 2022

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Journal articles on the topic "Relaxation processes in nuclear magnetic resonance molecules"

1

Foster, Richard J., Robin A. Damion, Thomas G. Baboolal, Stephen W. Smye, and Michael E. Ries. "A nuclear magnetic resonance study of water in aggrecan solutions." Royal Society Open Science 3, no. 3 (2016): 150705. http://dx.doi.org/10.1098/rsos.150705.

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Aggrecan, a highly charged macromolecule found in articular cartilage, was investigated in aqueous salt solutions with proton nuclear magnetic resonance. The longitudinal and transverse relaxation rates were determined at two different field strengths, 9.4 T and 0.5 T, for a range of temperatures and aggrecan concentrations. The diffusion coefficients of the water molecules were also measured as a function of temperature and aggrecan concentration, using a pulsed field gradient technique at 9.4 T. Assuming an Arrhenius relationship, the activation energies for the various relaxation processes

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2

Sellies, Lisanne, Ruud L. E. G. Aspers, and Marco Tessari. "Determination of hydrogen exchange and relaxation parameters in PHIP complexes at micromolar concentrations." Magnetic Resonance 2, no. 1 (2021): 331–40. http://dx.doi.org/10.5194/mr-2-331-2021.

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Abstract. Non-hydrogenative para-hydrogen-induced polarization (PHIP) is a fast, efficient and relatively inexpensive approach to enhance nuclear magnetic resonance (NMR) signals of small molecules in solution. The efficiency of this technique depends on the interplay of NMR relaxation and kinetic processes, which, at high concentrations, can be characterized by selective inversion experiments. However, in the case of dilute solutions this approach is clearly not viable. Here, we present alternative PHIP-based NMR experiments to determine hydrogen and hydride relaxation parameters as well as t

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3

Yagihara, Shin, Hironobu Saito, Hironori Sugimoto, et al. "Evaluation of water structures in cotton cloth by fractal analysis with broadband dielectric spectroscopy." Journal of Materials Science 56, no. 31 (2021): 17844–59. http://dx.doi.org/10.1007/s10853-021-06419-7.

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AbstractBroadband dielectric spectroscopy measurements were performed on naturally dried cotton cloth, and a recently developed analytical technique for fractal analysis of water structures was applied to obtain existential states and locations of water molecules in the material. Three relaxation processes observed in GHz, MHz, and kHz frequency regions were attributed to dynamic behaviors of hydrogen bonding networks (HBNs) of water and interacting molecules, polymer chains with interacting ion and water molecules, and ions restricted on the interfaces of larger structures, respectively. Wate

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4

Rampino, Sergio, Mirco Zerbetto, and Antonino Polimeno. "Stochastic Modelling of 13C NMR Spin Relaxation Experiments in Oligosaccharides." Molecules 26, no. 9 (2021): 2418. http://dx.doi.org/10.3390/molecules26092418.

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A framework for the stochastic description of relaxation processes in flexible macromolecules including dissipative effects has been recently introduced, starting from an atomistic view, describing the joint relaxation of internal coordinates and global degrees of freedom, and depending on parameters recoverable from classic force fields (energetics) and medium modelling at the continuum level (friction tensors). The new approach provides a rational context for the interpretation of magnetic resonance relaxation experiments. In its simplest formulation, the semi-flexible Brownian (SFB) model h

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5

Hronský, V., J. Murín, and J. Uhrin. "Dynamic-mechanical and nuclear magnetic resonance study of relaxation processes in ultra-high molecular weight polyethylene fibres." Czechoslovak Journal of Physics 56, no. 3 (2006): 289–302. http://dx.doi.org/10.1007/s10582-006-0089-3.

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6

Martini, Silvia, Claudia Bonechi, Alberto Foletti, and Claudio Rossi. "Water-Protein Interactions: The Secret of Protein Dynamics." Scientific World Journal 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/138916.

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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 prope

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7

Lim, Ae Ran. "Molecular dynamics of hybrid halide perovskite (CH3NH3)2CuX4 (X = Br and Cl) determined by nuclear magnetic resonance relaxation processes." Solid State Sciences 96 (October 2019): 105955. http://dx.doi.org/10.1016/j.solidstatesciences.2019.105955.

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8

Yamada, Shunji, Atsushi Kurotani, Eisuke Chikayama, and Jun Kikuchi. "Signal Deconvolution and Noise Factor Analysis Based on a Combination of Time–Frequency Analysis and Probabilistic Sparse Matrix Factorization." International Journal of Molecular Sciences 21, no. 8 (2020): 2978. http://dx.doi.org/10.3390/ijms21082978.

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Nuclear magnetic resonance (NMR) spectroscopy is commonly used to characterize molecular complexity because it produces informative atomic-resolution data on the chemical structure and molecular mobility of samples non-invasively by means of various acquisition parameters and pulse programs. However, analyzing the accumulated NMR data of mixtures is challenging due to noise and signal overlap. Therefore, data-cleansing steps, such as quality checking, noise reduction, and signal deconvolution, are important processes before spectrum analysis. Here, we have developed an NMR measurement informat

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9

Weisenberger, L. A., and J. L. Koenig. "NMR Imaging of Solvent Diffusion in Polymers." Applied Spectroscopy 43, no. 7 (1989): 1117–26. http://dx.doi.org/10.1366/0003702894203453.

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Nuclear magnetic resonance (NMR) imaging is sensitive to the mobile protons of solvent molecules and, as such, is well suited for studying the solvent diffusion in polymers. The fundamentals of NMR imaging are described, providing a platform for application of NMR imaging to diffusion processes in polymers. The constraints on the imaging experiment imposed by the diffusion process are discussed with respect to sample geometry and the rate of diffusion. A fast imaging scheme known as FLASH is described as an alternative method which reduces the influence of the diffusion rate and NMR relaxation

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10

Anthis, Nicholas J., and G. Marius Clore. "Visualizing transient dark states by NMR spectroscopy." Quarterly Reviews of Biophysics 48, no. 1 (2015): 35–116. http://dx.doi.org/10.1017/s0033583514000122.

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AbstractMyriad biological processes proceed through states that defy characterization by conventional atomic-resolution structural biological methods. The invisibility of these ‘dark’ states can arise from their transient nature, low equilibrium population, large molecular weight, and/or heterogeneity. Although they are invisible, these dark states underlie a range of processes, acting as encounter complexes between proteins and as intermediates in protein folding and aggregation. New methods have made these states accessible to high-resolution analysis by nuclear magnetic resonance (NMR) spec

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