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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...
Subviral Agents01:29

Subviral Agents

Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
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

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Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

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Related Experiment Video

Updated: Jul 19, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Copper and the prion protein: methods, structures, function, and disease.

Glenn L Millhauser1

  • 1Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA. glennm@chemistry.ucsc.edu

Annual Review of Physical Chemistry
|November 2, 2006
PubMed
Summary

Transmissible spongiform encephalopathies (TSEs) are linked to prion protein (PrP(C)) conversion. New research highlights copper

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases.
  • These diseases result from the misfolding and aggregation of the prion protein (PrP).
  • The normal cellular prion protein is denoted as PrP(C).

Purpose of the Study:

  • To review the recent findings on the interaction between copper and PrP(C).
  • To explore the role of copper in PrP(C) function and its implications in prion diseases.

Main Methods:

  • Electron paramagnetic resonance (EPR) spectroscopy was used to identify copper-binding sites.
  • Literature review of recent research connecting copper and PrP(C).

Main Results:

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High-throughput Screening for Protein-based Inheritance in S. cerevisiae

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

Published on: July 16, 2008

Related Experiment Videos

Last Updated: Jul 19, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

High-throughput Screening for Protein-based Inheritance in S. cerevisiae
08:12

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Published on: August 8, 2017

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

Interview: Protein Folding and Studies of Neurodegenerative Diseases

Published on: July 16, 2008

  • PrP(C) binds Cu(II) in its octarepeat domain.
  • EPR elucidated specific copper-binding sites within PrP(C).
  • Emerging evidence links copper dysregulation to prion disease pathogenesis.

Conclusions:

  • Copper binding is a key feature of PrP(C).
  • Understanding copper-PrP(C) interactions may offer insights into TSEs.
  • Further research into copper's role could reveal new therapeutic targets for prion diseases.