Related Experiment Video
Updated: Sep 30, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
Published on: October 23, 2016
Effect of hydrogen peroxide on the activity and structure of Escherichia coli chaperone GroEL
1Department of Biological Science and Biotechnology, Tsinghua University, Beijing, 100084 PR China.
Abstract:
Chaperone GroEL was treated with different concentrations of hydrogen peroxide. The conformational states of GroEL were monitored by protein intrinsic fluorescence, 8-anilino-1-naphthalene sulfonate fluorescence, and far-UV CD measurements. The results show that GroEL has unusual ability to resist oxidative stress. GroEL kept its quaternary structure and activity even when treated with 10 mM hydrogen peroxide. Two fragments were formed when GroEL was treated with high concentrations of hydrogen peroxide (more than 20 mM). It is suggested that GroEL, as a molecular chaperone, is related to oxidative process in vivo.
More Related Videos
07:14Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70
Published on: March 8, 2024
10:24Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Published on: June 7, 2018
Related Concept Videos
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Other Stress Responses in Bacteria
Stringent Response in E. coli