NR APAO
AU Wüthrich,K.; Bonjour,S.; Calzolai,L.; Gossert,A.; Güntert,P.; Hornemann,S.; Lührs,T.; Lysek,D.A.; Nivon,L.; Perez Lagos,D.
TI Species Variation of the Three-dimensional Structure of Cellular PrP
QU International Conference - Prion diseases: from basic research to intervention concepts - TSE-Forum, 08.10.-10.10.2003, Gasteig, München - Oral sessions OS-12
PT Konferenz-Vortrag
AB Using the method of nuclear magnetic resonance (NMR) spectroscopy in solution, the structures of the cellular form of the prion protein from various mammalian and non-mammalian species have been determined, as well as the structures of several variants of the human prion protein. This work was performed with recombinant prion proteins expressed in E. coli.. In this lecture, the prion proteins from the different species will be compared, and the structural similarities and differences will be analyzed with regard to the species barrier and the search for the so far unknown function of the cellular prion protein. The discussions will also include comparisons of the NMR spectra of the recombinant bovine prion protein produced in E. coli with prion protein isolated from bovine brain tissue.
AD Kurt Wüthrich, Sophie Bonjour, Luigi Calzolai, Alvar Gossert, Peter Güntert, Simone Hornemann, Thorsten Lührs, Dominikus A. Lysek, Lucas Nivon, Daniel Pérez Lagos, Swiss Federal Institute of Technology ETH Zürich
SP englisch
PO Deutschland