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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called 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...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called 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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

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Related Experiment Video

Updated: Jun 19, 2026

Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Prion protein misfolding.

L Kupfer1, W Hinrichs, M H Groschup

  • 1Department of Production Animal Health, Faculty of Veterinary Medicine, University of Calgary, 3330 Hospital Drive NW, Calgary, Alberta, T2N 4N1, Canada.

Current Molecular Medicine
|October 29, 2009
PubMed
Summary

Transmissible spongiform encephalopathies (TSEs) involve the misfolding of cellular prion protein (PrP(C)) into a disease-associated form (PrP(Sc)). Understanding this structural change is key to addressing neurodegenerative diseases.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Transmissible spongiform encephalopathies (TSEs) are linked to the misfolding of the host prion protein (PrP(C)) into an abnormal isoform (PrP(Sc)).
  • This conformational change initiates an autocatalytic process, leading to amyloid fibril accumulation in the CNS and neurodegeneration.

Purpose of the Study:

  • To review the structural aspects of prion protein misfolding.
  • To identify key protein regions involved in the PrP(C) to PrP(Sc) conformational transition.
  • To compare prion protein characteristics with other proteins that form insoluble fibrils.

Main Methods:

  • Literature review focusing on structural biology and protein-protein interactions.
  • Analysis of existing data on prion protein structure and misfolding pathways.
  • Comparative analysis of prion protein with other amyloidogenic proteins.

Main Results:

  • The review highlights specific protein regions potentially crucial for the PrP(C) to PrP(Sc) conversion.
  • It emphasizes the lack of understanding regarding the exact molecular mechanisms driving this conformational change.
  • Comparison with other fibril-forming proteins aims to elucidate unique aspects of prion diseases.

Conclusions:

  • Further research into the structural determinants of prion protein misfolding is essential.
  • Understanding the conformational transition is critical for developing therapeutic strategies against TSEs.
  • Comparative studies may offer insights into the fundamental principles of protein misfolding and aggregation.