Related Experiment Video
Updated: Aug 15, 2026

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain
Published on: October 3, 2012
The scrapie fibril protein and its cellular isoform
Abstract:
Proteins need help to fold and attain their functional conformation (Ellis and Hemmingsen 1989), and mechanisms have evolved to prevent the accumulation of misfolded protein aggregates within cells (Pelham 1988). These mechanisms fail to prevent the formation of protease-resistant, misfolded forms of PrP (ScPrP) during the development of scrapie and other transmissible spongiform encephalopathies, and ScPrP is a biochemical marker of these diseases. Much is now known about the structure and expression of the PrP gene, but the physiological function of the PrP protein and the mechanism by which the TDE pathogen replicates and specifically interferes with PrP metabolism remain a mystery--a mystery which will entertain prion-ophiliacs for some time yet.
More Related Videos
12:57Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
Published on: January 8, 2015
09:43Purification and Refolding to Amyloid Fibrils of (His)6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli
Published on: December 19, 2015
Related Concept Videos
RNA Splicing
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Leaky Scanning
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Subviral Agents