The Structural Transition of the Prion Protein into its Pathogenic Conformation is Induced by Unmasking Hydrophobic Sites

The Structural Transition of the Prion Protein into its Pathogenic Conformation is Induced by Unmasking Hydrophobic Sites

A series of structural intermediates in the putative pathway from the cellular prion protein PrP C to the pathogenic form PrP Sc was established by systematic variation of low concentrations (

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Bibliographische Detailangaben
Veröffentlicht in:Journal of molecular biology 2004-11, Vol.344 (3), p.839-853
Hauptverfasser: Leffers, K.-W., Schell, J., Jansen, K., Lucassen, R., Kaimann, T., Nagel-Steger, L., Tatzelt, J., Riesner, D.
Format: Artikel
Sprache:eng
Schlagworte:
Binding Sites
chaperonin
Circular Dichroism
conformation
Electrophoresis, Polyacrylamide Gel
prion
Protein Conformation
PrPSc Proteins - chemistry
PrPSc Proteins - metabolism
PrPSc Proteins - pathogenicity
SDS
Sodium Dodecyl Sulfate - chemistry
Solubility
Spectrometry, Fluorescence
transition
Ultracentrifugation
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Beschreibung
Zusammenfassung:A series of structural intermediates in the putative pathway from the cellular prion protein PrP C to the pathogenic form PrP Sc was established by systematic variation of low concentrations (
ISSN:0022-2836
1089-8638
DOI:10.1016/j.jmb.2004.09.071