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Interaction of selected divalent metal ions with human ataxin-3 Q36

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Interaction of selected divalent metal ions with human ataxin-3 Q36

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dc.contributor.author Stawoska, Iwona pl
dc.contributor.author Wesełucha-Birczyńska, Aleksandra [SAP11011404] pl
dc.contributor.author Regonesi, Maria Elena pl
dc.contributor.author Riva, Matteo pl
dc.contributor.author Tortora, Paolo pl
dc.contributor.author Stochel, Grażyna [SAP11011061] pl
dc.date.accessioned 2015-02-17T19:02:36Z
dc.date.available 2015-02-17T19:02:36Z
dc.date.issued 2009 pl
dc.identifier.issn 0949-8257 pl
dc.identifier.uri http://ruj.uj.edu.pl/xmlui/handle/item/3155
dc.language eng pl
dc.title Interaction of selected divalent metal ions with human ataxin-3 Q36 pl
dc.type JournalArticle pl
dc.description.physical 1175-1185 pl
dc.abstract.en The mode of interaction of ataxin-3 Q36 (AT-3 Q36) with selected endogenous and exogenous metal ions, namely, Zn^{2+}, Cu^{2+}, Ni^{2+}, and Cd^{2+}, was examined. Metal-ion-induced structural changes of the protein were monitored by fluorescence as well as Fourier transform Raman spectroscopy. We found that the cations tested lead to a decrease in α-helical content and a concurrent increase in β-sheet as well as undefined (β-turn and random-coil) structures. The most evident effect was observed for copper and nickel cations. After titration with these cations, the AT3 Q36 secondary structure content (27% α-helices in the presence of either ion, 31 and 27% β-sheets for Cu^{2+} and Ni^{2+}, respectively) was similar to that observed for the aggregated form of the protein (27% α-helices, 36% β-sheets). Using the 1-anilinonaphthalene-8-sulfonate hydrophobic fluorescence probe, we showed that the presence of the metal ions tested led to the formation of solvent-exposed hydrophobic patches of AT-3 Q36, and that such an effect decreased with increasing ionic radius. pl
dc.subject.en ataxin-3 pl
dc.subject.en Fourier transform Raman pl
dc.subject.en metal ions pl
dc.subject.en secondary structures pl
dc.description.volume 14 pl
dc.description.number 8 pl
dc.identifier.doi 10.1007/s00775-009-0561-1 pl
dc.identifier.eissn 1432-1327 pl
dc.title.journal JBIC. Journal of Biological Inorganic Chemistry pl
dc.language.container eng pl
dc.affiliation Wydział Chemii : Zakład Chemii Nieorganicznej pl
dc.affiliation Wydział Chemii : Zakład Fizyki Chemicznej pl
dc.subtype Article pl


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