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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...
Mismatch Repair01:20

Mismatch Repair

Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...
Mismatch Repair01:36

Mismatch Repair

Overview
Mismatch Repair01:36

Mismatch Repair

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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...

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Related Experiment Video

Updated: Jul 7, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
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Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

Molecular chaperones and selection against mutations.

Katarzyna Tomala1, Ryszard Korona

  • 1Institute of Environmental Sciences, Jagiellonian University, Gronostajowa 7, 30-387 Krakow, Poland. katarzyna.tomala@uj.edu.pl

Biology Direct
|February 27, 2008
PubMed
Summary

Molecular chaperones can either help or hinder mutated proteins. Their dual role in protein folding and degradation impacts genetic variation and adaptation, with implications for evolution.

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Intracellular Refolding Assay
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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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Related Experiment Videos

Last Updated: Jul 7, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
06:55

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

Intracellular Refolding Assay
07:18

Intracellular Refolding Assay

Published on: January 24, 2012

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

Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Genetics

Background:

  • Molecular chaperones stabilize proteins under stress.
  • Chaperones may maintain activity of mutated proteins, masking deleterious effects and allowing genetic variation accumulation.
  • This variation could facilitate adaptation during environmental changes.

Purpose of the Study:

  • To review studies on chaperone interactions with mutated proteins.
  • To investigate the dual role of chaperones in protein stabilization versus degradation.
  • To assess the impact of chaperones on protein evolution and evolvability.

Main Methods:

  • Literature review focusing on studies of chaperone-mutated polypeptide interactions.
  • Analysis of experimental evidence from bacterial and eukaryotic systems.
  • Examination of chaperone roles in protein folding, degradation, and cellular regulation.

Main Results:

  • Chaperones can alleviate mutation effects by assisting destabilized proteins, particularly in bacteria with chaperone overexpression.
  • In eukaryotes, chaperone malfunction exacerbates mutation effects, likely via deregulation of cellular systems.
  • Evidence suggests some chaperones (e.g., Hsp90-dependent) can target unstable mutated proteins for degradation, exposing mutations.

Conclusions:

  • The net effect of chaperones on mutated proteins (assistance vs. degradation) is currently unclear due to limited experimental data.
  • Chaperones may either accelerate or decelerate protein sequence evolution depending on their predominant role.
  • Chaperones, particularly Hsp90, are complex regulators of evolvability, with potential antagonistic roles impacting protein stability and aggregation.