Structural Properties of Recombinant Human Prion Protein
Priori diseases are a group of fatal, neurodegenerative conditions affecting both humans and animals. Previously called transmissible spongiform encephalopathies or slow virus diseases they are unique in that they may have a sporadic, inherited or transmissible origin. The transmissible prion diseases have become an area of increasing public concern because of the epidemic of a novel bovine prion disease, bovine spongiform encephalopathy, and despite recent advances, many uncertainties exist in understanding of the nature of the infectious agent.
KeywordsPrion Protein Prion Disease Bovine Spongiform Encephalopathy Guanidine Hydrochloride NOESY Spectrum
Unable to display preview. Download preview PDF.
- Pan, K., Baldwin, M.A., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Huang, Z., Fletterick, R.J., Cohen, F.E., and Prusiner, S.B. (1993). Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 90, 10962–10966.PubMedCrossRefGoogle Scholar
- Safar, J., Wang, W., Padgett, M.P., Ceroni, M., Piccardo, P., Zopf, D., Gajdusek, D.C., and Gibbs, C.J.J. (1990). Molecular mass, biochemical composition, and physicochemical behavior of the infectious form of the scrapie precursor protein monomer. Proc. Natl. Acad. Sci. U. S. A. 87, 6373–6377.PubMedCrossRefGoogle Scholar
- Staniforth, R.A., Burston, S.G., Smith, C.J., Jackson, G.S., Badcoe, I.G., Atkinson, T., Holbrook, J.J. and Clarke, A.R. (1993). The energetics and cooperativiry of protein folding. A simple experimental analysis based upon the solvation of internal residues. Biochemistry 32, 3842–3851.PubMedCrossRefGoogle Scholar