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Related Concept Videos

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...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
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...

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Related Experiment Video

Updated: Jun 2, 2026

Interview: Protein Folding and Studies of Neurodegenerative Diseases
19:50

Interview: Protein Folding and Studies of Neurodegenerative Diseases

Published on: July 16, 2008

Prions and protein-folding diseases.

E Norrby1

  • 1Center for the History of Science, Royal Swedish Academy of Sciences, Stockholm, Sweden. erling.norrby@kva.se

Journal of Internal Medicine
|April 13, 2011
PubMed
Summary
This summary is machine-generated.

Prions are misfolded proteins causing fatal neurodegenerative diseases like Creutzfeldt-Jakob disease (CJD). Understanding prion propagation is key to combating these and other protein-misfolding disorders.

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Last Updated: Jun 2, 2026

Interview: Protein Folding and Studies of Neurodegenerative Diseases
19:50

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Published on: July 16, 2008

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09:18

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Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Protein Chemistry

Background:

  • Prions are misfolded proteins that propagate by inducing conformational changes in normal proteins.
  • These abnormal isoforms aggregate into pathogenic amyloid structures.
  • Prion diseases, or transmissible spongiform encephalopathies (TSEs), are lethal neurodegenerative conditions affecting humans and animals.

Purpose of the Study:

  • To review the evolution of the prion concept and its underlying molecular mechanisms.
  • To summarize historical and recent findings on prion disease transmission and pathogenesis.
  • To explore the broader implications of protein misfolding and aggregation in neurodegenerative diseases.

Main Methods:

  • Review of historical literature and scientific publications on prions and TSEs.
  • Analysis of documented transmission routes of human and animal prion diseases.
  • Synthesis of recent research on protein aggregation mechanisms and their link to other neurodegenerative conditions.

Main Results:

  • The prion concept originated from understanding information transfer between homologous proteins, independent of nucleic acids.
  • Key human prion diseases include kuru and Creutzfeldt-Jakob disease (CJD), linked to animal scrapie.
  • Epidemics of bovine spongiform encephalopathy (BSE) and variant CJD resulted from contaminated feed and meat consumption, now controlled by public health measures.

Conclusions:

  • Prion diseases highlight the dangers of protein misfolding and inter-protein communication.
  • The mechanisms of prion aggregation are relevant to common neurodegenerative diseases like Alzheimer's and Parkinson's.
  • Prion protein aggregation may play a physiological role in neuronal function and memory formation.