|Kehrli Jr, Marcus|
Submitted to: Association of Analytical Communities International Midwest Section
Publication Type: Abstract Only
Publication Acceptance Date: 4/9/2005
Publication Date: 5/24/2005
Citation: Nicholson, E.M., Greenlee, J.J., Richt, J., Hamir, A.N., Kunkle, R.A., Kehrli, Jr., M.E. 2005. Biochemistry of prion diseases. Association of Analytical Communities International, Midwest Section [abstract]. Abstract No. 601. p. 38.
Technical Abstract: The nucleation-polymerization and template assistance models for conversion of the normal cellular form of the prion protein, PrP**C, to the disease associated, protease resistant conformation, PrP**d, will be discussed. Attention will be paid to a recent model of PrP**d fibril structure, the implications such a conformation has on the inactivation of prion infectivity, and the methods to detect inactivation.