The prion protein is a copper binding glycoprotein that in mammals can misfold into a pathogenic isoform leading to prion diseases, as opposed, surprisingly, to avians. The avian prion N-terminal tandem repeat is richer in prolines than the mammal one, and understanding their effect on conformation is of great biological importance. Here we succeeded in investigating the conformations of a single avian hexarepeat by means of NMR and molecular dynamics techniques. We found a high flexibility and a strong conformational dependence on pH: local turns are present at acidic and neutral pH, while unordered regions dominate at basic conditions.
Autori interni: | |
Autori: | PIETROPAOLO A; RAIOLA L; MUCCIOLI L; TIBERIO G; ZANNONI C; FATTORUSSO R; ISERNIA C; LA MENDOLA D; PAPPALARDO G; RIZZARELLI E |
Titolo: | An NMR and Molecular Dynamics investigation of the avian prion hexarepeat conformational features in solution |
Anno del prodotto: | 2007 |
Digital Object Identifier (DOI): | 10.1016/j.cplett.2007.05.046 |
Appare nelle tipologie: | 1.1 Articolo in rivista |