Repozytorium
Wyszukaj
Kolekcje
Inne
Molecular dynamics study of the Cu2+ binding-induced "structuring" of the N-terminal domain of human prion protein.
Autorzy
Rok wydania
2009
Czasopismo
Journal of Physical Chemistry B
Numer woluminu
113
Strony
3277-3279
DOI
10.1021/jp901030a
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
In this work, we report molecular dynamics simulations on a fragment of the human prion protein spanning residues 31−120, with copper(II) bound to the repeat region in several ways corresponding to the known intra- and inter-repeat coordination modes, or to the metal site located at His111. The results of this study point to a different structuring tendency of the protein fragment depending on copper binding mode, with the highest degree of structuring in the case of intrarepeat Cu(II) coordination corresponding to high copper concentration.
Adres publiczny
https://doi.org/10.1021/jp901030a
Strona internetowa wydawcy
Podobne publikacje
The complex-formation behaviour of His residues in the fifth Cu2+ binding site of human prion protein: a close look.
Remelli Maurizio, Valensin Daniela, Bacco D., Gralka Ewa K., Guerrini Remo, Migliorini Caterina, Kozłowski Henryk
Impact of SDS surfactant on the interactions of Cu2+ ions with the amyloidogenic region of human prion protein.
Hecel Aleksandra, Migliorini Caterina, Valensin Daniela, Łuczkowski Marek, Kozłowski Henryk
Thermodynamic and spectroscopic investigation on the role of met residues in CuII binding to the non-octarepeat site of the human prion protein.
Remelli Maurizio, Valensin Daniela, Toso Leonardo, Gralka Ewa K., Guerrini Remo, Marzola Erika, Kozłowski Henryk