Nuclear Magnetic Resonance Spectroscopy in Solutions

Most of our structural information comes from x-ray crystallographic analysis of protein crystals and from the use of nuclear magnetic resonance spectroscopy in solution. Each of these techniques has advantages and limitations which makes them suitable for a complementary range of problems. The first protein structure determined at a sufficient resolution to trace the path of the polypeptide chain was that of myoglobin in 1960. Since that time many thousands of structures corresponding to hundreds of different proteins have been determined. The coordinates of the atoms in many protein and nucleic acid structures are available from the Protein Data Bank, which may be accessed via the Internet or World Wide Web (http //www.pdb.bnl.gov). 

R145 J. Garcia, L. G. Martins and M. Pons, Nuclear Magnetic Resonance Spectroscopy in Solution , in Supramolecular Chemistry From Molecules to Nanomaterials, eds. P. A. Gale and J. W. Steed, John Wiley Sons Ltd., Chichester, UK, 2012, Vol. 2, p. 297. 

Solution Mass spectroscopy is a technique used to deter-mine the molecular weight, formula and structure of a compound. It differs from infrared, raman, ultraviolet and nuclear magnetic resonance spectroscopy in that it is a destructive spectroscopy the sample is fragmented by the technique and cannot be recovered in its original form. Mass spectroscopy involves the bombardment of a sample with an electron beam of a particular energy. If the sample is subjected to a low energy electron beam (about 10 eV-electron volts) the molecule will lose an electron to... 

Hall LD. Solutions to the hidden-resonance problem in proton nuclear magnetic resonance spectroscopy. Adv Carbohydr Chem Biochem 1974 29 11—40. Hall LD. High-resolution nuclear magnetic resonance spectroscopy. In Pigman W, Horton D, eds. The Carbohydrates, Chemistry and Biochemistry. Academic Press, New York, 1980 Vol. IB 1299-1326. 

Wiithrich, K. Protein structure determination in solution by nuclear magnetic resonance spectroscopy. Science 243 45-50, 1989. 

Nuclear magnetic resonance spectroscopy of the solutes in clathrates and low temperature specific heat measurements are thought to be particularly promising methods for providing more detailed information on the rotational freedom of the solute molecules and their interaction with the host lattice. The absence of electron paramagnetic resonance of the oxygen molecule in a hydroquinone clathrate has already been explained on the basis of weak orientational effects by Meyer, O Brien, and van Vleck.18... 

In either dilute or concentrated solutions, additional reactions occur that result in both intra- and intermolecular cross-linking of proteins. There is little direct chemical information from such techniques as nuclear magnetic resonance spectroscopy or mass spectrometry to detail the precise nature of these cross-links.5,6... 

Partington, P., Feeney, J. and Burgen, A. S. V. The conformation of acetylcholine and related compounds in aqueous solutions as studied by nuclear magnetic resonance spectroscopy. Mol. Pharmacol. 8 269-277,1972. 

Turner BL, Richardson AE. Identification of scyllo-inositol phosphates in soil by solution phosphorus-31 nuclear magnetic resonance spectroscopy. Soil Sci. Soc. Am. J. 2004 68 802-808. 

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... 

Fushman, D. and D. Cowburn, Nuclear magnetic resonance relaxation in determination of residue-specific 1SN chemical shift tensors in proteins in solution protein dynamics, structure, and applications of transverse relaxation optimized spectroscopy, in Methods Enzymol. T. James, U. Schmitz, and V. Doetsch, Editors. 2001. p.109-126. 

For the pressure studies, two phase" compact ion behavior is observed with an inflection point between 7 and 11 atms. For the aqueous solution studies, the hydraulic permeability K and the g-ratio are hardly effected by solute type (within experimental error). The solute diffusive permeability however, varies with solute type in good qualitative agreement with free energy parameters, infrared overtone shifts, and spin echo and continuous wave nuclear magnetic resonance spectroscopy results from the literature. 

Nuclear magnetic resonance spectroscopy of dilute polymer solutions is utilized routinely for analysis of tacticlty, of copolymer sequence distribution, and of polymerization mechanisms. The dynamics of polymer motion in dilute solution has been investigated also by protoni - and by carbon-13 NMR spectroscopy. To a lesser extent the solvent dynamics in the presence of polymer has been studied.Little systematic work has been carried out on the dynamics of both solvent and polymer in the same systan. 

Nuclear magnetic resonance spectroscopy is the most powerful technique for the determination of the structure of intermolecular complexes in solution... 

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