Zoroddu, Maria Antonietta and Peana, Massimiliano Francesco and Medici, Serenella (2006) Structural changes induced by nickel binding to the N-tail of Histone H4: an NMR study. In: EuChemMS 1. European chemistry congress, 27-31 agosto 2006, Budapest, Hungary. p. 392. ISBN 963-9319-61-9. Conference or Workshop Item.
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Carcinogenicity of certain nickel compounds has been confirmed by the combination of epidemiological evidence in humans and carcinogenesis bioassays in animals. We have previously reported that nickel is a potent suppressor of histone H4 acetylation in both yeast and mammalian cells. We have recently carried out a study on the coordination ability of Ni(I1) to the N-terminal tail of histone H4 by the use of multidimensional NMR techniques (ID, 2D TOCSY and NOESY spectra) [I]. The data thus collected allowed us to calculate a structural model for the square planar complex formed by the Ni(I1) ion and ow peptide, pointing out the important structural changes induced by nickel coordination on the peptide.
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