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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...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

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Related Experiment Video

Updated: Jul 18, 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

[The non-functioning chaperonin GroEL stimulates protein aggregation].

I N Naletov, E V Shmal'gauzen, I N Shalova

    Biomeditsinskaia Khimiia
    |December 22, 2006
    PubMed
    Summary

    Chaperonins like GroEL play a role in amyloid diseases by binding prions. Functionally inactive chaperonins accelerate prion aggregation, forming amyloid structures.

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    Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor

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    Last Updated: Jul 18, 2026

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

    Published on: June 7, 2018

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    Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor

    Published on: June 29, 2021

    Area of Science:

    • Protein folding and aggregation
    • Neurodegenerative diseases
    • Molecular chaperones

    Context:

    • Amyloid diseases are linked to protein misfolding and aggregation.
    • Chaperonins, such as GroEL, assist in protein folding.
    • The role of chaperonins in prion disease pathogenesis is not fully understood.

    Purpose:

    • To investigate the interaction between the chaperonin GroEL and misfolded proteins, specifically prions.
    • To determine how prions affect chaperonin-assisted protein folding.
    • To elucidate the role of chaperonins in amyloid aggregate formation.

    Summary:

    • Prions bind to GroEL, reducing its efficiency in folding denatured glyceraldehyde-3-phosphate dehydrogenase (GAPDH).
    • Inactive GroEL (GroEL/GroES without Mg-ATP) bound prions, forming large aggregates (>400 nm).
    • Mg-ATP addition reduced aggregate size (70-80 nm), while blocked chaperonin centers increased aggregation (1200 nm).

    Impact:

    • Chaperonins significantly influence amyloid structure formation.
    • Functionally inactive chaperonins accelerate protein aggregation, contributing to amyloid diseases.
    • The findings provide a model for evaluating anti-aggregation compounds in chaperone-containing systems.