Related Experiment Video
Updated: Jun 1, 2026

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
Published on: April 13, 2022
Double mutant MBP refolds at same rate in free solution as inside the GroEL/GroES chaperonin chamber when aggregation
Navneet K Tyagi1, Wayne A Fenton, Ashok A Deniz
1Howard Hughes Medical Institute, Yale School of Medicine, New Haven, CT 06510, USA.
Abstract:
Under "permissive" conditions at 25°C, the chaperonin substrate protein DM-MBP refolds 5-10 times more rapidly in the GroEL/GroES folding chamber than in free solution. This has been suggested to indicate that the chaperonin accelerates polypeptide folding by entropic effects of close confinement. Here, using native-purified DM-MBP, we show that the different rates of refolding are due to reversible aggregation of DM-MBP while folding free in solution, slowing its kinetics of renaturation: the protein exhibited concentration-dependent refolding in solution, with aggregation directly observed by dynamic light scattering. When refolded in chloride-free buffer, however, dynamic light scattering was eliminated, refolding became concentration-independent, and the rate of refolding became the same as that in GroEL/GroES. The GroEL/GroES chamber thus appears to function passively toward DM-MBP.
More Related Videos
08:32Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
Published on: October 23, 2016
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
Molecular Chaperones and Protein Folding
The...
Molecular Chaperones and Protein Folding
The...
Bacterial Protein Maturation
Protein Folding Quality Check in the RER
Export of Misfolded Proteins out of the ER
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...