Prion protein amyloid formation involves structural rearrangements in C-terminal domain

TitlePrion protein amyloid formation involves structural rearrangements in C-terminal domain
Publication TypeJournal Article
Year of Publication2010
AuthorsKumar J, Sreeramulu S, Schmidt T-L, Richter C, Vonck J, Heckel A, Glaubitz C, Schwalbe H
JournalChemBioChem
Volume11
Pagination1208-1213
Accession Number188
Abstract

We have analyzed the structural rearrangements of the urea-denatured state of recombinant prion protein by using liquid-state NMR spectroscopy. Our studies document that prion amyloid fibrils generated from monomeric, urea-unfolded human prion protein have a rigid core between residues 145-223.
URLhttp://www3.interscience.wiley.com/journal/123429247/abstract
DOIDOI: 10.1002/cbic.201000076