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The role of hydroxyl group of tyrosine in copper(II) binding by His-analogs of oxytocin.
Autorzy
Rok wydania
2013
Czasopismo
Numer woluminu
396
Strony
40-48
DOI
10.1016/j.ica.2012.09.035
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
In this paper we report on the interaction between the Cu(II) ions and the histidine analogues of oxytocin. The studied His-analogues are characterized by presence of Tyr2 or Phe2 amino acid residues and free or protected N-terminal group. The use of potentiometric methods allowed for the determination of the stoichiometry of formed complexes and calculation of their stability constants. The number of spectroscopic measurements (UV–Vis, CD, NMR, fluorescence) together with the theoretical calculation enabled to obtain the structures of formed complexes and the influence of Tyr2 amino acid residue on the efficiency of metal ion binding.
Słowa kluczowe
oxytocin, copper, Complex, histidine
Adres publiczny
http://dx.doi.org/10.1016/j.ica.2012.09.035
Strona internetowa wydawcy
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