title: Molecular dynamics study of the Cu2+ binding-induced "structuring" of the N-terminal domain of human prion protein.
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.
authors.forename: Gianni
authors.initials: G
authors.lastname: Valensin
authors.forename: Elena
authors.initials: E
authors.lastname: Molteni
authors.forename: Daniela
authors.initials: D
authors.lastname: Valensin
authors.forename: Magdalena
authors.initials: M
authors.lastname: Taraszkiewicz
authors.forename: Henryk
authors.initials: H
authors.lastname: Kozlowski
mesh_terms: D003198:Computer Simulation; D003300:Copper / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry; D006801:Humans; D021962:Membrane Microdomains / Q000737:chemistry; D008958:Models, Molecular; D011328:Prions / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D011328:Prions; D006639:Histidine; D003300:Copper