Reversible Conversion of Monomeric Human Prion Protein between Native and Fibrilogenic Conformations

Prion propagation involves the conversion of cellular prion protein (PrP$^C$) into a disease-specific isomer, PrP$^{Sc}$, shifting from a predominantly α-helical to β-sheet structure. Here, conditions were established in which recombinant human PrP could switch between the native α conformation, cha...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 1999-03, Vol.283 (5409), p.1935-1937
Hauptverfasser:	Jackson, G. S., Hosszu, L. L. P., Power, A., Hill, A. F., Kenney, J., Saibil, H., Craven, C. J., Waltho, J. P., Clarke, A. R., Collinge, J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetates Analytical, structural and metabolic biochemistry Biochemistry Biological and medical sciences Circular Dichroism Endopeptidase K - metabolism Fundamental and applied biological sciences. Psychology Gels Holoproteins Humans Hydrogen-Ion Concentration Molecular biology Molecular Weight Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Other proteins Oxidation-Reduction Physiological aspects Prion diseases Prions Prions (Proteins) Prions - chemistry Protein Conformation Protein Folding Protein isoforms Protein Isoforms - chemistry Protein Structure, Secondary Protein Structure, Tertiary Proteins PrPC Proteins - chemistry PrPSc Proteins - chemistry Recombinant Proteins - chemistry Sodium Solar fibrils Solubility Spectrum Analysis
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