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Sökning: WFRF:(McIntyre Deane D.)

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1.
  • Murari, A., et al. (författare)
  • A control oriented strategy of disruption prediction to avoid the configuration collapse of tokamak reactors
  • 2024
  • Ingår i: Nature Communications. - 2041-1723 .- 2041-1723. ; 15:1
  • Tidskriftsartikel (refereegranskat)abstract
    • The objective of thermonuclear fusion consists of producing electricity from the coalescence of light nuclei in high temperature plasmas. The most promising route to fusion envisages the confinement of such plasmas with magnetic fields, whose most studied configuration is the tokamak. Disruptions are catastrophic collapses affecting all tokamak devices and one of the main potential showstoppers on the route to a commercial reactor. In this work we report how, deploying innovative analysis methods on thousands of JET experiments covering the isotopic compositions from hydrogen to full tritium and including the major D-T campaign, the nature of the various forms of collapse is investigated in all phases of the discharges. An original approach to proximity detection has been developed, which allows determining both the probability of and the time interval remaining before an incoming disruption, with adaptive, from scratch, real time compatible techniques. The results indicate that physics based prediction and control tools can be developed, to deploy realistic strategies of disruption avoidance and prevention, meeting the requirements of the next generation of devices.
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2.
  • Thomas, HS, et al. (författare)
  • 2019
  • swepub:Mat__t
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5.
  • McIntyre, Deane D., et al. (författare)
  • Nitrogen-14 NMR relaxation, and reorientation behavior of dissolved dinitrogen
  • 1989
  • Ingår i: Journal of magnetic resonance. - : Elsevier BV. - 1090-7807 .- 1096-0856 .- 0022-2364. ; 83:2, s. 377-382
  • Tidskriftsartikel (refereegranskat)abstract
    • In recent years, nitrogen- 14 and - 15 NMR spectroscopy has become an important technique in organic chemistry and in biochemistry ( Z-4). A frequent occurrence in the NMR spectra of both nuclei is the presence of a signal at approximately -7 1.5ppm (referred to neat nitromethane; -66 ppm referred to aqueous nitrate). This resonance, which has been observed in water (4) and a range of organic solvents (.5-7), has been the subject of some confusion in the literature. In the case of nitrogen-14 NMR spectra, the signal for the quadrupolar nucleus has a remarkably narrow linewidth (about 25 Hz) compared to those recorded for a wide variety of other substances. This indicates a fairly high degree of electronic symmetry about the nitrogenatom and/or a very short correlation time ( 7,). In a recent report (8)) this signal has been assigned to dissolved dinitrogen on the basis that it could be removed by degassing´the solution; however, no reference was made to the fact that it had a remarkably narrow linewidth compared to other 14N NMR resonances. When detected in the 15NCIDNP spectra of the decomposition products of diazonium ions (5, 6) as well as azo compounds ( 7)) the signal has been assigned either to dinitrogen (6, 7) or to a terminal diazonium nitrogen (5). This work is in general agreement with our own observations over a period of years which indicate that the signal arises from dissolved dinitrogen. We have measured the 14N chemical shift of dissolved N2 in a number of solvents at 25°C and have also determined the T, and T2 relaxation times under a variety of conditions in solvents of different viscosity. This Note is concerned with a discussion of these 14N NMR observations and with the determination of the correlation time of dissolved dinitrogen which permits the determination of both the enthalpy and the entropy of activation via the Eyring equation. These results will be compared with earlier reported data regarding the chemical shift and relaxation of liquid nitrogen obtained under a variety of conditions ( 9-12). All spectra were obtained on a Bruker AM-400 wide-bore NMR spectrometer operating in the FT mode at a frequency of 28.9 MHz for 14N and 40.5 MHz for 15N, using a 10 mm broadband probe. Typical conditions for the acquisition of 14N spectra
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6.
  • Weininger, Ulrich, et al. (författare)
  • Specific (CD2CD2SCHD2)-C-12-D-beta-C-12-D-gamma-C-13-H-epsilon Isotopomer Labeling of Methionine To Characterize Protein Dynamics by H-1 and C-13 NMR Relaxation Dispersion
  • 2012
  • Ingår i: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 1520-5126 .- 0002-7863. ; 134:45, s. 18562-18565
  • Tidskriftsartikel (refereegranskat)abstract
    • Protein dynamics on the micro- to millisecond time scale is increasingly found to be critical for biological function, as demonstrated by numerous NMR relaxation dispersion studies. Methyl groups are excellent probes of protein interactions and dynamics because of their favorable NMR relaxation properties, which lead to sharp signals in the H-1 and C-13 NMR spectra. Out of the six different methyl-bearing amino acid residue types in proteins; methionine plays a special role because of its extensive side chain flexibility and the high polarizability of the sulfur atom. Methionine is over-represented:in many protein-protein recognition sites making the methyl group of this, residue type an important probe of the relationships among dynamics, Interactions, and biological function. Here we present a straightforward method to label methionine residues with specific (CHD2)-C-13 methyl isotopomers against a deuterated background. The resulting protein samples yield NMR spectra with improved sensitivity due to the essentially 100% population of the desired (CHD2)-C-13 methyl isotopomer, which is ideal for H-1 and C-13 spin relaxation experiments to investigate protein dynamics in general and conformational exchange in particular. We demonstrate the approach by measuring H-1 and C-13 CPMG relaxation dispersion for the nine methionines in calcium free calmodulin (apo-CaM). The results. show that the C- terminal domain, but not the N-terminal domain, of apo-CaM undergoes fast exchange between the ground state and a high-energy state. Since target proteins are known to bind specifically to the C-terminal domain of apo-CaM, we speculate that the high energy state might be involved in target binding through conformational selection.
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