Nuclear magnetic resonance spectroscopy carbon 13 relaxation

Oldfield, E., Norton, R. S., and Allerhand, A. (1975)./. Biol. Chem. 250, 6368. Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon-13 Nuclear Magnetic Resonance Spectroscopy. Relaxation Behavior. 

Pearson, H., Gust, D., Armitage, I. M., Huber, H., Roberts, J. D., Stark, R. E., Void, R. R., and Void, R. L. (1975). Proc. Nat. Acad. Sci. U.S.A. 72, 1599. Nuclear Magnetic Resonance Spectroscopy Reinvestigation of Carbon-13 Spin-Lattice Relaxation Time Measurements of Amino Acids. 

Several spectroscopic techniques, namely, Ultraviolet-Visible Spectroscopy (UV-Vis), Infrared (IR), Nuclear Magnetic Resonance (NMR), etc., have been used for understanding the mechanism of solvent-extraction processes and identification of extracted species. Berthon et al. reviewed the use of NMR techniques in solvent-extraction studies for monoamides, malonamides, picolinamides, and TBP (116, 117). NMR spectroscopy was used as a tool to identify the structural parameters that control selectivity and efficiency of extraction of metal ions. 13C NMR relaxation-time data were used to determine the distances between the carbon atoms of the monoamide ligands and the actinides centers. The II, 2H, and 13C NMR spectra analysis of the solvent organic phases indicated malonamide dimer formation at low concentrations. However, at higher ligand concentrations, micelle formation was observed. NMR studies were also used to understand nitric acid extraction mechanisms. Before obtaining conformational information from 13C relaxation times, the stoichiometries of the... 

Oldfield, E., and A. Allerhand Identification of Tryptophan Resonance in Natural Abundance Carbon-13 Nuclear Magnetic Resonance Spectra of Proteins. Application of Partially Relaxed Fourier Trasform Spectroscopy. J. Amer. Chem. Soc. 97, 221-224 (1975). 

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