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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...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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.
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Protein Folding01:22

Protein Folding

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Related Experiment Video

Updated: May 13, 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

Chaperone activation by unfolding.

Linda Foit1, Jenny S George, Bin W Zhang

  • 1Howard Hughes Medical Institute and Department of Chemistry and Biophysics Program, University of Michigan, Ann Arbor, MI 48109-1055, USA.

Proceedings of the National Academy of Sciences of the United States of America
|March 15, 2013
PubMed
Summary
This summary is machine-generated.

Some proteins activate by unfolding. Researchers mutated the HdeA protein, finding a version active at neutral pH, demonstrating activation through partial unfolding.

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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: May 13, 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

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

  • Biochemistry
  • Molecular Biology
  • Protein Folding

Background:

  • Conditionally disordered proteins exhibit dynamic conformational changes.
  • Protein function is typically linked to ordered states, but some proteins activate upon unfolding.
  • HdeA, a periplasmic chaperone, is crucial for bacterial survival in acidic environments like the stomach.

Purpose of the Study:

  • To investigate the mechanism of HdeA activation.
  • To determine if partial unfolding can directly activate a protein.
  • To engineer an HdeA mutant active at neutral pH.

Main Methods:

  • Site-directed mutagenesis of HdeA to alter pH-dependent monomerization.
  • Biochemical assays to assess chaperone activity and protein stability.
  • Conformational analysis of wild-type and mutant HdeA.

Main Results:

  • A mutant HdeA protein was generated that is active at neutral pH.
  • This mutant HdeA is destabilized, partially unfolded, and monomeric at neutral pH.
  • The mutant HdeA effectively prevents substrate protein aggregation at neutral pH.

Conclusions:

  • Partial unfolding can directly activate a protein.
  • HdeA activation is linked to its monomerization and partial unfolding.
  • This study provides evidence for a novel mechanism of protein activation.