Heteronuclear magnetic resonance

Powers, R., Garrett, D.S., March, C.l. et al. (1992). Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy. Science 256, 1673. 

H. Sfihi, C. Rey, 1-D and 2-D Double heteronuclear magnetic resonance study of the local structure of type B carbonate fluorapatite, in J. Fraissard, B. Lapina (Eds.), Magnetic Resonance in Colloid and Interface Science, Nato ASI Series II, Vol. 76, Kluwer Academic Publishers, Dordrecht, 2002, pp. 409-422. 

Vis, H., Boelens, R., Mariani, M., Stroop, R., Vorgias, C. E., Wilson, K. S., Kaptein, R. (1994). H, C, and N resonance assignments and secondary structure analysis of the HU protein from Bacillus stearothermophilus using two-and three-dimensional double- and triple-resonance heteronuclear magnetic resonance spectroscopy. Biochemistry 33, 14858-14870. 

GM Clore, AM Gronenborn. Determination of structures of larger proteins in solution by three- and four-dimensional heteronuclear magnetic resonance spectroscopy. In GM Clore, AM Gronenborn, eds. NMR of Proteins. Boca Raton, FL CRC Press, 1993, pp. 1-32. 

Similarly, heteronuclear magnetic resonance spectroscopy with nuclei of spins 1/2... 

The isomeric o-, m-, and /7-carbaboranes and their EtsSn derivatives have been examined by H- B heteronuclear magnetic resonance techniques to obtain accurate proton chemical-shift and coupling-constant data. ... 

Heteronuclear Magnetic Resonance Applications to Biological and Related Paramagnetic Molecules... 

A polyfluorooxometalate complex, [Ni(H20)NaH2Wi7055F6] has been employed in the epoxidation reactions with hydrogen peroxide. This Ni-substituted TMSP has been used as a catalyst for the oxidation of cis-cyclohexene in a two-phase system of DCF/H2O at 60°C obtaining the corresponding epoxide with >99% selectivity and quantitative yield. The stability of the complex has been assessed by FTIR, atomic absortion and heteronuclear magnetic resonance ( F-NMR) measurements. Formation of the intermediate oxo/peroxo species has been observed by FTIR analysis. ... 

A. M. Gronenborn and G. M. Clore, Crit. Rev. Biochem. Mol. Biol., 30, 351 (1995). Structures of Protein Complexes by Multidimensional Heteronuclear Magnetic Resonance Spectroscopy. 

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... 

Nuclear magnetic resonance (NMR) has proved to be a very useful tool for structural elucidation of natural products. Recent progress in the development of two-dimensional 1H- and 13C-NMR techniques has contributed to the unambiguously assignment of proton and carbon chemical shifts, in particular in complex molecules. The more used techniques include direct correlations through homonuclear (COSY, TOCSY, ROESY, NOESY) [62-65] and heteronuclear (HMQC, HMBC) [66. 67] couplings. 

In 1969, the possibility of determining 119Sn chemical shifts of organotin compounds was increased when McFarlane and coworkers (7) suggested the H- 119Sn heteronuclear double magnetic resonance (HDMR) method, based on the use of H NMR spectra. 

Fig. 8. Heteronuclear single-quantum coherenc (HSQC) spectrum of the hypothetical protein of the flowering locus T protein produced in the cell-free system. The FT protein was synthesized in the same way as in Fig. 6 except that Ala, Leu, Gly, and Gin in both translation and substrate mixture were replaced with their -labeled forms (Isotec, Inc ). After incubation for 48 h, the reaction mixture (1 mL) was dialyzed against 10 mMphosphate buffer (pH 6.5) overnight, and then centrifuged at 30,000g for 10 min. The supernatant containing 30 xMof the protein was directly subjected to nuclear magnetic resonance spectroscopy. The spectrum was recorded on a Broker DMX-500 spectrometer at 25°C, and 2048 scans were averaged for the final H- WHSQC spectrum.

This chapter describes protocols for preparing 15N-labeled proteins (ubiquitin is used as an example) using Escherichia coli cells (with purification) and the wheat germ cell-free system (without purification). A comparison of I I-15N heteronuclear single-quantum coherence (HSQC) spectra of yeast ubiquitin prepared using each method indicates that this wheat germ cell-free system may be used for rapid nuclear magnetic resonance analyses of proteins without purification. 

Finally, I am pleased to mention the review on heteronuclear magnetic double resonance by Dr W. McFarlane and Dr D. S. Rycroft which updates the thorough reviews by Dr McFarlane presented in Volumes 1 and 5A. 

Clore GM, et al. Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy. Biochemistry 1990 29 7387-7401. Aue WP, Bartholdi E, Ernst RR. Two-dimensional spectroscopy. Application to nuclear magnetic resonance. J. Chem. Phys. 1976 64 p. 2229-2246. 

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. 

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