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Relaxation Time Measurements (relaxation + time_measurement)
Selected AbstractsProbing the Local Structure of Pure Ionic Liquid Salts with Solid- and Liquid-State NMR,CHEMPHYSCHEM, Issue 1 2010Peter G. Gordon Abstract Room-temperature ionic liquids (RTILs) are gaining increasing interest and are considered part of the green chemistry paradigm due to their negligible vapour pressure and ease of recycling. Evidence of liquid-state order, observed by IR and Raman spectroscopy, diffraction studies, and simulated by ab initio methods, has been reported in the literature. Here, quadrupolar nuclei are used as NMR probes to extract information about the solid and possible residual order in the liquid state of RTILs. To this end, the anisotropic nature and field dependence of quadrupolar and chemical shift interactions are exploited. Relaxation time measurements and a search for residual second-order quadrupolar coupling were employed to investigate the molecular motions present in the liquid state and infer what kind of order is present. The results obtained indicate that on a timescale of ,10,8 sec or longer, RTILs behave as isotropic liquids without residual order. [source] NMR-Solution Structures and Affinities for the Human Somatostatin G-Protein-Coupled Receptors hsst1,5 of CF3 Derivatives of Sandostatin® (Octreotide)HELVETICA CHIMICA ACTA, Issue 12 2009Dieter Seebach Abstract The previously reported (Helv. Chim. Acta2008, 91, 2035) derivatives of octreotide (1) with a (CF3)-Trp substitution, i.e., 3, and with open-chain structures, i.e., 2, 4, and 5, have been tested for their affinities to hsst1,5 receptors and subjected to a detailed NMR analysis. Their affinities vary from 15,nM to 5,,M, as compared to 0.6,nM to 0.8,,M for octreotide itself (Table,1). This decreased bioactivity may have had to be expected for the open-chain compounds 4 and 5; possible reasons for this decrease in the case of CF3 derivative of octreotide, 3, are discussed. NMR Analysis (Tables,2 and 3) provides evidence for increased dynamics of all new derivatives 2,5. The dynamics of the octreotide molecule 1 was analyzed by (natural-abundance) longitudinal 13C-T1 -relaxation time measurements (Table,4), from which the conclusion is drawn that the backbone of the macrocycle is rather rigid on the time scale of this method. [source] Routine clinical brain MRI sequences for use at 3.0 TeslaJOURNAL OF MAGNETIC RESONANCE IMAGING, Issue 1 2005Hanzhang Lu PhD Abstract Purpose To establish image parameters for some routine clinical brain MRI pulse sequences at 3.0 T with the goal of maintaining, as much as possible, the well-characterized 1.5-T image contrast characteristics for daily clinical diagnosis, while benefiting from the increased signal to noise at higher field. Materials and Methods A total of 10 healthy subjects were scanned on 1.5-T and 3.0-T systems for T1 and T2 relaxation time measurements of major gray and white matter structures. The relaxation times were subsequently used to determine 3.0-T acquisition parameters for spin-echo (SE), T1 -weighted, fast spin echo (FSE) or turbo spin echo (TSE), T2 -weighted, and fluid-attenuated inversion recovery (FLAIR) pulse sequences that give image characteristics comparable to 1.5 T, to facilitate routine clinical diagnostics. Application of the routine clinical sequences was performed in 10 subjects, five normal subjects and five patients with various pathologies. Results T1 and T2 relaxation times were, respectively, 14% to 30% longer and 12% to 19% shorter at 3.0 T when compared to the values at 1.5 T, depending on the region evaluated. When using appropriate parameters, routine clinical images acquired at 3.0 T showed similar image characteristics to those obtained at 1.5 T, but with higher signal-to-noise ratio (SNR) and contrast-to-noise ratio (CNR), which can be used to reduce the number of averages and scan times. Recommended imaging parameters for these sequences are provided. Conclusion When parameters are adjusted for changes in relaxation rates, routine clinical scans at 3.0 T can provide similar image appearance as 1.5 T, but with superior image quality and/or increased speed. J. Magn. Reson. Imaging 2005;22:13,22. © 2005 Wiley-Liss, Inc. [source] Method for quantitative imaging of the macromolecular 1H fraction in tissuesMAGNETIC RESONANCE IN MEDICINE, Issue 5 2003Stefan Ropele Abstract A new method was developed for mapping the relative density of the macromolecular protons involved in magnetization transfer (MT). This method employs a stimulated echo preparation scheme in order to modulate the phase distribution within a spin ensemble. This labeled spin ensemble is then used as an intrinsic indicator, which is diluted due to magnetization exchange with macromolecular protons. A pulse sequence is presented which compensates for longitudinal relaxation, allows observation of the dilution effect only, and provides for calculation of parameter maps using indicator dilution theory. Compared to other quantitative MT techniques, neither additional relaxation time measurements nor knowledge regarding the lineshape of the macromolecular proton pool are required. Moreover, the inherent low specific absorption rate and the low sensitivity for B1 errors make this method favorable in a clinical setting. This sequence was used to measure the macromolecular proton density in cross-linked bovine serum albumin. Using a navigated echo planar readout, the sequence was also employed to visualize the macromolecular content of human brain in vivo. Magn Reson Med 49:864,871, 2003. © 2003 Wiley-Liss, Inc. [source] Complex 1H,13C-NMR relaxation and computer simulation study of side-chain dynamics in solid polylysineBIOPOLYMERS, Issue 3 2005Alexey Krushelnitsky Abstract The side-chain dynamics of solid polylysine at various hydration levels was studied by means of proton spin,lattice relaxation times measurements in the laboratory and tilted (off-resonance) rotating frames at several temperatures as well as Monte Carlo computer simulations. These data were analyzed together with recently measured carbon relaxation data (A. Krushelnitsky, D. Faizullin, and D. Reichert, Biopolymers, 2004, Vol. 73, pp. 1,15). The analysis of the whole set of data performed within the frame of the model-free approach led us to a conclusion about three types of the side-chain motion. The first motion consists of low amplitude rotations of dihedral angles of polylysine side chains on the nanosecond timescale. The second motion is cis,trans conformational transitions of the side chains with correlation times in the microsecond range for dry polylysine. The third motion is a diffusion of dilating defects described in (W. Nusser, R. Kimmich, and F. Winter, Journal of Physical Chemistry, 1988, Vol. 92, pp. 6808,6814). This diffusion causes almost no reorientation of chemical bonds but leads to a sliding motion of side chains with respect to each other in the nanosecond timescale. This work evidently demonstrates the advantages of the simultaneous quantitative analysis of data obtained from different experiments within the frame of the same mathematical formalism, providing for the detailed description of the nature and geometry of the internal molecular dynamics. © 2005 Wiley Periodicals, Inc. Biopolymers 78: 129,139, 2005 This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com [source] | |||||||||||||