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The binding of aluminium ion to [Leu5]-enkephalin has been investigated by 1H, 13C and 27Al NMR spectroscopy in dimethyl sulphoxide solution at different peptide/metal ratio. Analysis of the spectra suggests that Al3+ binds at two metal-binding sites. The binding of Al3+ at the first site involves the Tyr1CO, and Leu5COO- groups to give a 2:1 species in a(More)
The influence of aluminum ions introduced either directly or with sorbitol, in collagen and skin, has been investigated by Thermally Stimulated Current/TSC spectroscopy. The intramolecular mobility of collagen has been found to be significantly reduced by aluminum ions. The substitution of water molecules by aluminum ions on intramolecular hydrophilic sites(More)
Interaction of Cu(II) and Gly-His-Lys, a growth-modulating tripeptide from plasma, was investigated by 13C- and 1H-n.m.r. and e.p.r. spectroscopy. The n.m.r. line-broadening was interpreted in terms of major and minor species formed as a function of pH. The results indicate that the n.m.r. line-broadening is due to the presence of minor species in rapid(More)
A sensitive and reliable method for the atomic-absorption spectrometric determination of micro-amounts of Ni in organic and inorganic samples has been developed, with separation of nickel by carbonyl generation. Foreign anions and cations do not interfere. Only metallic iron hampers the generation of Ni(CO)(4) but this interference can be avoided if the(More)
The nonapeptide less than Glu-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn (formerly called serum thymic factor) is a factor produced by the thymic epithelium, which needs a zinc ion to express its immunoregulatory properties. We report here on 1H and 13C NMR investigation of the conformational properties of the free peptide in aqueous medium and in dimethyl(More)
Interaction of Zn2+ with thymulin was investigated by 1H NMR spectroscopy. In DMSO-d6 solution, Zn2+ forms a complex with a nonapeptide involving the C-terminal carboxylate and the hydroxyl groups of the two serine residues in position 4 and 8, in a tetrahedral structure.
Two enkephalin analogues, Tyr-D-Ala-Gly-Phe-NVal-NH2 and Tyr-D-Ala-Gly-Phe-NVal-OH were studied by n.m.r. spectroscopy. 13C chemical shifts were determined as a function of pH and in water-dimethyl sulfoxide solvent mixtures. The acid and amide forms of the analogues show a marked difference in their n.m.r. features. Complexation with metal ions causes(More)