Title of article
The role of hydroxyl group of tyrosine in copper(II) binding by His-analogs of oxytocin
Author/Authors
Kotynia، نويسنده , , Aleksandra and Czy?nikowska، نويسنده , , ?aneta and Cebrat، نويسنده , , Marek and Jaremko، نويسنده , , ?ukasz and G?adysz، نويسنده , , Olimpia and Jaremko، نويسنده , , Mariusz and Marciniak، نويسنده , , Aleksandra and Brasu?، نويسنده , , Justyna، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2013
Pages
9
From page
40
To page
48
Abstract
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.
Keywords
Oxytocin , Complex , Copper , histidine
Journal title
INORGANICA CHIMICA ACTA
Serial Year
2013
Journal title
INORGANICA CHIMICA ACTA
Record number
1331691
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