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Molecular Chaperones and Protein Folding

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.
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Updated: Oct 20, 2025

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

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DsbA is a redox-switchable mechanical chaperone.

Edward C Eckels^1,2, Deep Chaudhuri³, Soham Chakraborty³

¹Department of Biological Sciences, Columbia University New York NY 10027 USA ece7001@nyp.org.

Chemical Science

|September 15, 2021

Summary

This summary is machine-generated.

DsbA, a bacterial oxidoreductase, exhibits redox-controlled chaperone activity, promoting protein folding and reducing translocation energy costs. Its oxidation state fine-tunes this chaperone function.

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

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Published on: October 23, 2016

Area of Science:

Microbiology
Biochemistry
Molecular Biology

Background:

DsbA is a key bacterial oxidoreductase involved in protein folding.
Its precise role in protein translocation and folding remains incompletely understood.

Purpose of the Study:

To investigate the redox-controlled chaperone activity of DsbA.
To elucidate the relationship between DsbA's oxidation state and its chaperone function.
To quantify the impact of DsbA-assisted folding on protein translocation energetics.

Main Methods:

Magnetic tweezers-based single-molecule force spectroscopy was employed.
Independent measurements of oxidoreductase activity and chaperone behavior were performed.
A seven-residue peptide was used to map the DsbA chaperone binding site.

Main Results:

DsbA demonstrates redox-controlled chaperone activity for both cysteine-containing and cysteine-free substrates.
Oxidized DsbA significantly promotes protein folding, an effect diminished upon reduction of the CXXC motif.
A specific peptide identified the chaperone binding site on DsbA.
DsbA-assisted periplasmic protein folding reduces ATP consumption for translocation by up to 33%.

Conclusions:

DsbA functions as a redox-sensitive chaperone, influencing protein folding and translocation.
The oxidation state of DsbA is critical for its chaperone efficacy.
DsbA-mediated folding provides a mechanical work output that enhances translocation efficiency.