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Gradient Spin-echo (gradient + spin-echo)
Selected Abstracts7Li, 31P, and 1H Pulsed Gradient Spin-Echo (PGSE) Diffusion NMR Spectroscopy and Ion Pairing: On the Temperature Dependence of the Ion Pairing in Li(CPh3), Fluorenyllithium, and Li[N(SiMe3)2] amongst Other SaltsCHEMISTRY - A EUROPEAN JOURNAL, Issue 5 2005Ignacio Fernández Abstract 7Li, 31P, and 1H variable-temperature pulsed gradient spin-echo (PGSE) diffusion methods have been used to study ion pairing and aggregation states for a range of lithium salts such as lithium halides, lithium carbanions, and a lithium amide in THF solutions. For trityllithium (2) and fluorenyllithium (9), it is shown that ion pairing is favored at 299 K but the ions are well separated at 155 K. For 2-lithio-1,3-dithiane (13) and lithium hexamethyldisilazane (LiHMDS 16), low-temperature data show that the ions remain together. For the dithio anion 13, a mononuclear species has been established, whereas for the lithium amide 16, the PGSE results allow two different aggregation states to be readily recognized. For the lithium halides LiX (X = Br, Cl, I) in THF, the 7Li PGSE data show that all three salts can be described as well-separated ions at ambient temperature. The solid state structure of trityllithium (2) is described and reveals a solvent-separated ion pair formed by a [Li(thf)4]+ ion and a bare triphenylmethide anion. [source] Analysis of b -value calculations in diffusion weighted and diffusion tensor imagingCONCEPTS IN MAGNETIC RESONANCE, Issue 1 2005Daniel Güllmar Abstract Diffusion weighted imaging has opened new diagnostic possibilities by using microscopic diffusion of water molecules as a means of image contrast. The directional dependence of diffusion has led to the development of diffusion tensor imaging, which allows us to characterize microscopic tissue geometry. The link between the measured NMR signal and the self-diffusion tensor is established by the so-called b matrices that depend on the gradient's direction, strength, and timing. However, in the calculation of b -matrix elements, the influence of imaging gradients on each element of the b matrix is often neglected. This may cause errors, which in turn leads to an incorrect extraction of diffusion coefficients. In cases where the imaging gradients are high (high spatial resolution), these errors may be substantial. Using a generic pulsed gradient spin-echo (PGSE) imaging sequence, the effects of neglecting the imaging gradients on the b -matrix calculation are demonstrated. By measuring an isotropic phantom with this sequence it can be analytically as well as experimentally shown that large deviations in single b -matrix elements are generated. These deviations are obtained by applying the diffusion weighting in the readout direction of the imaging dimension in combination with relatively large imaging gradients. The systematic errors can be avoided by a full b -matrix calculation considering all the gradients of the sequence or by generating cross-term free signals using the geometric average of two diffusion weighted images with opposite polarity. The importance of calculating the exact b matrices by the proposed methods is based on the fact that more precise diffusion parameters are obtained for extracting correct property maps, such as fractional anisotropy, volume ratio, or conductivity tensor maps. © 2005 Wiley Periodicals, Inc. Concepts Magn Reson Part A 25A: 53,66, 2005 [source] Improved resolution in two-dimensional 1H NMR spectra of peptides by band-selective, homonuclear decoupling during both the evolution and acquisition periods: application to characterization of the binding of peptides by heparinMAGNETIC RESONANCE IN CHEMISTRY, Issue 8 2006Jing Wang Abstract Two-dimensional 1H NMR experiments that achieve band-selective, homonuclear decoupling in both the indirectly detected F1 and directly detected F2 dimensions were used to assign the highly overlapped 1H NMR spectrum of the peptide Ac-SRGKARVRAKVKDQTK-NH2, both free in solution and bound to heparin. Band-selective, homonuclear decoupling during the evolution period was achieved using a double pulsed field gradient spin-echo (DPFGSE) with semi-selective shaped pulses; band-selective, homonuclear decoupling during the acquisition period was achieved by time-shared semi-selective shaped pulse decoupling. Regular TOCSY, ROESY and NOESY spectra and TOCSY, ROESY and NOESY spectra measured with band-selective, homonuclear decoupling in the evolution (F1) dimension (BASHD-TOCSY, ROESY and NOESY spectra) and with band-selective, homonuclear decoupling in both the F1 and F2 dimensions (D-(or Double)-BASHD-TOCSY, ROESY and NOESY spectra) are reported and compared for the peptide and its heparin complex. Complete assignment of the 1H-NMR spectra of the free and heparin-complexed peptide was achieved with the high resolution of the D-BASHD-TOCSY, ROESY and NOESY spectra. Characterization of the heparin-complexed peptide is of interest because of the ability of the peptide to neutralize the anticoagulant activity of heparin. Copyright © 2006 John Wiley & Sons, Ltd. [source] Practical aspects of ROESY experiments for identification of bound waters in the cyclic tetrasaccharideMAGNETIC RESONANCE IN CHEMISTRY, Issue 12 2005Kazuo Furihata Abstract ROESY pulse sequences are presented and evaluated to identify bound waters in the cyclic tetrasaccharide. The first experiment incorporated the double-pulsed field gradient spin-echo (DPFGSE) for selective water excitation at the initial portion of the pulse sequence. Although long, shaped pulses were used in DPFGSE to achieve the highly selective excitation of water resonance that is very close to resonances of the cyclic tetrasaccharide, the approach was not effective because of the loss of sensitivity. Concomitant use of long delays and moderate length of shaped pulses in the portion of DPFGSE gained more sensitivity. A simple approach incorporating spin-echo with long delays instead of DPFGSE also afforded a sensitive spectrum. Practical aspects of these ROESY experiments are illustrated using the cyclic tetrasaccharide cyclo -{,6}-,- D -Glcp -(1,3)-,- D -Glcp -(1,6)-,- D -Glcp -(1,3)-,- D -Glcp -(1,). Copyright © 2005 John Wiley & Sons, Ltd. [source] 7Li, 31P, and 1H Pulsed Gradient Spin-Echo (PGSE) Diffusion NMR Spectroscopy and Ion Pairing: On the Temperature Dependence of the Ion Pairing in Li(CPh3), Fluorenyllithium, and Li[N(SiMe3)2] amongst Other SaltsCHEMISTRY - A EUROPEAN JOURNAL, Issue 5 2005Ignacio Fernández Abstract 7Li, 31P, and 1H variable-temperature pulsed gradient spin-echo (PGSE) diffusion methods have been used to study ion pairing and aggregation states for a range of lithium salts such as lithium halides, lithium carbanions, and a lithium amide in THF solutions. For trityllithium (2) and fluorenyllithium (9), it is shown that ion pairing is favored at 299 K but the ions are well separated at 155 K. For 2-lithio-1,3-dithiane (13) and lithium hexamethyldisilazane (LiHMDS 16), low-temperature data show that the ions remain together. For the dithio anion 13, a mononuclear species has been established, whereas for the lithium amide 16, the PGSE results allow two different aggregation states to be readily recognized. For the lithium halides LiX (X = Br, Cl, I) in THF, the 7Li PGSE data show that all three salts can be described as well-separated ions at ambient temperature. The solid state structure of trityllithium (2) is described and reveals a solvent-separated ion pair formed by a [Li(thf)4]+ ion and a bare triphenylmethide anion. [source] | ||||||||||