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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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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.
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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
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Related Experiment Video

Updated: Nov 6, 2025

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Structural determinants of multimerization and dissociation in 2-Cys peroxiredoxin chaperone function.

Laura Troussicot1, Björn M Burmann1, Mikael Molin2

  • 1Department of Chemistry and Molecular Biology, University of Gothenburg, 405 30 Göteborg, Sweden; Wallenberg Centre for Molecular and Translational Medicine, University of Gothenburg, 405 30 Göteborg, Sweden.

Structure (London, England : 1993)
|May 4, 2021
PubMed
Summary

Peroxiredoxins (PRDXs), known peroxidases, also function as molecular chaperones. This review details structural insights into 2-Cys PRDXs, revealing how their structure facilitates chaperone activity and interacts with other chaperones.

Keywords:
2-Cys peroxiredoxinHsp40chaperone functiondissociationholdase activityoligomerizationsmall heat shock protein

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Peroxiredoxins (PRDXs) are ubiquitous peroxidases with recently identified molecular chaperone functions.
  • Understanding the structural basis of this dual role is crucial for cell biology.

Purpose of the Study:

  • To review structural studies of 2-Cys PRDX systems that exhibit chaperone activity.
  • To elucidate the structural determinants and mechanisms underlying PRDX chaperone function.

Main Methods:

  • Analysis of existing structural data on 2-Cys PRDXs.
  • Comparison of PRDX structures with other molecular chaperones.

Main Results:

  • PRDXs modulate their quaternary structure to interact with client proteins.
  • Structural similarities exist between 2-Cys PRDXs, small heat shock proteins (HSPs), and Hsp40 holdases.

Conclusions:

  • The structure of PRDXs is key to their chaperone activity.
  • PRDXs share functional and structural principles with other chaperone families, particularly regarding oligomerization states.