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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 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

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Articles linked to this work by shared authors, journal, and citation graph.

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Folding on the chaperone: yield enhancement through loose binding.

Journal of molecular biology·2006
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Free energy landscapes for amyloidogenic tetrapeptides dimerization.

Biophysical journal·2005
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Accelerated folding in the weak hydrophobic environment of a chaperonin cavity: creation of an alternate fast folding pathway.

Proceedings of the National Academy of Sciences of the United States of America·2004
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Improved theoretical description of protein folding kinetics from rotations in the phase space of relevant order parameters.

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Kinetics of the coil-to-helix transition on a rough energy landscape.

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Related Experiment Video

Updated: Jul 8, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
08:32

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Published on: October 23, 2016

Do chaperonins boost protein yields by accelerating folding or preventing aggregation?

A I Jewett1, J-E Shea

  • 1Department of Chemistry and Biochemistry, University of California, Santa Barbara, California, USA.

Biophysical Journal
|January 15, 2008
PubMed
Summary
This summary is machine-generated.

The GroEL/ES chaperonin

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

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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

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Last Updated: Jul 8, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
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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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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

Area of Science:

  • Molecular Biology
  • Biophysics
  • Protein Folding

Background:

  • The GroEL/ES chaperonin system facilitates protein folding.
  • Its function is debated: unfoldase activity versus acting as a protective cage.
  • Aggregation is a major pathway for protein degradation.

Purpose of the Study:

  • To investigate the role of GroEL's unfoldase activity in preventing protein aggregation.
  • To model the effect of increased chaperonin cycle frequency on protein folding yields.

Main Methods:

  • Development of a simple kinetic model.
  • Simulation of a hypothetical GroEL mutation increasing ATP hydrolysis rate.

Main Results:

  • Increased chaperonin cycle frequency paradoxically increases protein aggregation.
  • Faster cycles lead to more time in the bulk, enhancing aggregation risk.
  • The unfoldase function is critical for preventing aggregation under these conditions.

Conclusions:

  • The unfoldase activity of GroEL is crucial for efficient protein folding, especially when aggregation is prevalent.
  • Accelerating the chaperonin cycle can be counterproductive, reducing overall folding yields.
  • This highlights the delicate balance in chaperonin-assisted protein folding.