NMR spectroscopy magnetic resonance

Bruhn H, Frahm J, Gyngell ML et at (1989). Cerebral metabolism in man after acute stroke new observations using localized proton NMR spectroscopy. Magnetic Resonance Medicine 9 126-131 Calautti C, Naccarato M, Jones PS et at (2007). The relationship between motor deficit and hemisphere activation balance after stroke a 3T fMRI study. Neuroimage 34 322-331... 

Christensen J. D., Babb, S. M., Cohen, B. M. and Renshaw, P. F. (1998) Quantitation of dexfen-fluramine/d-norfenfluramine concentration in primate brain using 19F NMR spectroscopy. Magnetic Resonance in Medicine, 39, 149-154. 

Choi I-Y, Tkac I, and Gruetter R (2000) Single-shot, three-dimensional non-echo localisation method for in-vivo NMR spectroscopy. Magnetic Resonance in Medicine 44 387-394. 

Lindon JC, Farrant RD, Sanderson PN, et al. (1995) Separation and characterization of components of peptide libraries using on-flow coupled HPLC-NMR spectroscopy. Magnetic Resonance in Chemistry 33 857-863. 

Berners-Price SJ, Sadler PJ and Brevard C (1990) Tetrahedral, chelated, silver(I) diphosphine complexes. Rapid measurements of chemical shifts and couplings by two-dimensional P- ° Ag NMR spectroscopy. Magnetic Resonance in Chemistry 28 145-148. 

Translational motion occurs in liquid and gas phases of water, but is virtually eliminated in the solid phase (ice). Translational motion of water molecules can be measured using NMR and magnetic resonance imaging (MRI) spectroscopy (Sun and Schmidt, 1995). 

Non-specific sum parameter analysis [12,13], which is still used today, failed [14,15] in the analyses of some of these compounds. Chromatographic methods in combination with non-substance specific detectors, e.g. colorimetric and photometric [5] or with substance specific detectors such as IR (infrared spectroscopy), NMR (nuclear magnetic resonance spectroscopy) or MS (mass spectrometry), are applied increasingly nowadays. 

Figure 1.1 The electiomagnetic spectrum, showing the different microscopic excitation sources and the spectroscopies related to the different spectral regions. XRF, X-Ray Fluorescence AEFS, Absorption Edge Fine Structure EXAFS, Extended X-ray Absorption Fine Structure NMR, Nuclear Magnetic Resonance EPR, Electron Paramagnetic Resonance. The shaded region indicates the optical range.

Another method of determining the secondary and tertiary structure of a protein is NMR (nuclear magnetic resonance) spectroscopy. NMR spectroscopy reveals detailed information on specific sites of molecules without having to solve then-entire structure. 

NMR nuclear magnetic resonance NO-heme nitrosylheme NOESY nuclear Overhauser enhancement spectroscopy... 

The speed with which NMR spectroscopy has been incorporated into scientific inquiry is truly amazing. The first commercial spectrometers became available in the 1950s. By the middle 1980s whole bodies could be placed in the probes of NMR spectrometers (magnetic resonance imaging) and the structures of body parts could be determined in exquisite detail. Today structures of proteins and other macromolecules in solution or in the solid state are determined routinely. What was unthinkable in the 1960s is routinely practiced today even by undergraduates The power of the method and the structural detail it provides have no doubt fueled its rapid development. 

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