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:||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|