Multidimensional nuclear magnetic resonance

N. J. Heaton, C. Cao Minh, J. Kovats, U. Guru 2004, Saturation and Viscosity from Multidimensional Nuclear Magnetic Resonance Logging, SPE 90564 presented at SPE ATC E, Houston, TX, 26-29 September, 2004. 

Probably, one of the most valuable advances in this field has dealt with the first chemoenzymatic synthesis of the stable isotope-enriched heparin from a uniformly double labelled 13C, 15N /V-acetylheparosan from E. coli K5. Heteronuclear, multidimensional nuclear magnetic resonance spectroscopy was employed to analyze the chemical composition and solution conformation of N-acety 1 hcparosan, the precursors, and heparin. Isotopic enrichment was found to provide well-resolved 13C spectra with the high sensitivity required for conformational studies of these biomolecules. Stable isotope-labelled heparin was indistinguishable from heparin derived from animal tissues and might be employed as a novel tool for studying the interaction of heparin with different receptors.30... 

Lett., 81, 2727 (1998). Length Scale of Dynamic Heterogeneities at the Glass Transition Determined by Multidimensional Nuclear Magnetic Resonance. 

The possibilities of application of far-UV circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy in analysis of thermal stability of proteins and structural changes within protein molecules as well in explanation of cross reactivity between food allergens have been described in more detail in Section 3.4. Likewise nuclear magnetic resonance (NMR), especially 2D and multidimensional NMR as well as the method based on diffraction of monochromatic x-rays widely used in examination of tertiary structures of allergens have been described in Section 3.4 and by Neudecker et al. (2001) and Schirmer et al. (2005). 

The determination of the secondary and tertiary structure—that is, the details of the three-dimensional folding of the polypeptide chain of a protein at high resolution—relies on one of two powerful techniques x-ray diffraction analysis of protein crystals and multidimensional high-field nuclear magnetic resonance (NMR) spectroscopy. Both methods provide very detailed structural in-... 

From its very beginning nuclear magnetic resonance (NMR) was used to unravel dynamic processes in amorphous matter, where the high selectivity of this technique was exploited. Recent progress has largely benefited from the development of multidimensional NMR spectroscopy, significantly extending the traditional techniques such as spin-lattice relaxation and line-shape analyses. Modern NMR techniques helped a lot to understand the molecular dynamics in disordered systems such as the a-process. 

Sattler M, Schleucher J, Griesinger C. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Progress Nuclear Magnet. Reson. Spectros. 1999 34 93-158. 

Schmidt-Rohr, K. Spiess, H.W. (1994) Multidimensional Nuclear Magnetic Resonance and Polymers, Academic Press, London. 

There are more than 10,000 known sequences of proteins, but there are barely a thousand whose three dimensional (3D) structures have been determined, mostly by x-ray diffraction. With the development of multidimensional NMR (nuclear magnetic resonance) (Ernst et al., 1987) and the improvement in computing power, as well as the development of suitable computational algorithms, NMR spectroscopy has emerged as a second important method for structure determination of moderately sized proteins (up to M.W. 37,000 iJius far) in solution. 

R418 M. Krahk, B. Corain and M. Zecca, Catalysis by Metal Nanoparticles Supported on Functionalized Polymers , Chem. Pap., 2000, 54, 254 R419 Zh.A. Krasnaya, Dienone 2H-Pyran Valence Isomerization , Chem.-Heterocycl.Compd. (N. Y.), 1999, 35, 1255 R420 H.-M. Krenzlin, Dynamics of Complex Molecules and Multidimensional Nuclear Magnetic Resonance , Ber. Forschungszent. Juelich, 1999,(Juel-3726), i-iii, 1-125... 

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