Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5619
Title: Molecular dynamics study of the Cu2+ binding-induced "structuring" of the N-terminal domain of human prion protein
Authors: Valensin, Gianni 
Molteni, E
Valensin, Daniela 
Taraszkiewicz, M
Kozlowski, H.
Issue Date: 2009
Project: None 
Journal: JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL
Abstract: 
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.
Description: 
38147
URI: http://hdl.handle.net/20.500.12779/5619
ISSN: 1520-6106
DOI: 10.1021/jp901030a
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