Repozytorium
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Kolekcje
Inne
How non-bonding amino-acid side-chains may enormously increase the stability of a Cu(II) -peptide complex.
Autorzy
Rok wydania
1998
Czasopismo
Numer woluminu
283
Strony
1-11
DOI
10.1016/S0020-1693(98)00084-X
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
A combined pH-metric and spectroscopic (UV—Vis, circular dichroism and electron paramagnetic resonance) study of Cu(II) binding to analogues of Asn-Ser-Phe-Arg-Tyr-NH2 systematically substituted with Ala residues revealed the presence of indirect, additive conformational effects resulting in a very high stability enhancement for 4N complexes. The major contribution to the stability is exerted by non-binding side-chains of 4th and 5th amino acids. This effect is explained on the basis of spectroscopic data by the formation of a secondary fence shielding the Cu(II) binding site from the bulk of the solution. Such a structure, not reported previously, is of possible importance for the understanding of interactions of metal ions with proteins.
Słowa kluczowe
Copper complexes, Peptide complexes
Adres publiczny
https://doi.org/10.1016/S0020-1693(98)00084-X
Strona internetowa wydawcy
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