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|Title:||Molecular dynamics study of the Cu2+ binding-induced "structuring" of the N-terminal domain of human prion protein||Authors:||Valensin, Gianni
|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.
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