Molecular dynamics study of the Cu2+ binding-induced "structuring" of the N-terminal domain of human prion protein

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.