Publications

← Back
Journal/Book: ChemBioChem
Published: 2010
Pages: 1208-1213
Volume: 11
Issue:
Accession no.: 188
Publisher:
ISBN:

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

Jitendra Kumar, Sridhar Sreeramulu, Thorsten-Lars Schmidt, Christian Richter, Janet Vonck, Alexander Heckel, Clemens Glaubitz, Harald Schwalbe
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.
Imprint Privacy
© Copyright 2024
Prof. Dr. Harald Schwalbe
Institut für Organische Chemie und Chemische Biologie
Johann Wolfgang Goethe Universität
Max-von-Laue-Str. 7
D-60438 Frankfurt am Main
Website powered by