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Related Concept Videos

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...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
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...

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Related Experiment Video

Updated: Jun 23, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways.

Peter M Douglas1, Daniel W Summers, Douglas M Cyr

  • 1Department of Cell and Developmental Biology, School of Medicine, University of North Carolina, Chapel Hill, NC 27599-7090, USA.

Prion
|May 8, 2009
PubMed
Summary

Molecular chaperones can either promote or prevent protein aggregation, influencing the progression of neurodegenerative diseases. Understanding this dual role is key to developing new therapeutic strategies against toxic protein buildup.

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Protein misfolding and aggregation into amyloid plaques are hallmarks of neurodegenerative diseases.
  • Soluble oligomeric protein intermediates, not insoluble plaques, are increasingly recognized as the primary toxic species.
  • Molecular chaperones are critical regulators of protein homeostasis, influencing protein folding and degradation.

Purpose of the Study:

  • To investigate the multifaceted role of molecular chaperones in protein aggregation pathways.
  • To explore how chaperones modulate the formation of toxic soluble oligomers versus benign aggregates.
  • To understand chaperone-mediated mechanisms for suppressing neurotoxicity in proteinopathies.

Main Methods:

  • The study likely involves in vitro protein aggregation assays.
  • Biochemical analyses to characterize protein oligomers and aggregates.
  • Cellular models to assess chaperone effects on protein toxicity and neurodegeneration.

Main Results:

  • Chaperones can antagonize the aggregation of misfolded proteins, promoting refolding or degradation.
  • Evidence suggests chaperones can also convert toxic soluble oligomers into less harmful aggregates.
  • This chaperone activity influences the accumulation of proteotoxic soluble species.

Conclusions:

  • Molecular chaperones play a complex, dual role in protein aggregation, capable of both promoting and suppressing harmful assembly.
  • Chaperones represent a potential therapeutic target for neurodegenerative diseases by modulating protein aggregation.
  • Targeting chaperone activity could mitigate the neurotoxicity associated with soluble protein oligomers.