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
Link To Document :
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