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Journal/Book: ChemBioChem
Published: 2010
Pages: 1208-1213
Volume: 11
Accession no.: 188

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
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.
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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
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