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Updated: May 7, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
Published on: October 23, 2016
Rattling the cage: computational models of chaperonin-mediated protein folding
Jeremy England1, Del Lucent, Vijay Pande
1Department of Physics, Stanford University, United States.
Abstract:
Chaperonins are known to maintain the stability of the proteome by facilitating the productive folding of numerous misfolded or aggregation-prone proteins and are thus essential for cell viability. Despite their established importance, the mechanism by which chaperonins facilitate protein folding remains unknown. Computer simulation techniques are now being employed to complement experimental ones in order to shed light on this mystery. Here we review previous computational models of chaperonin-mediated protein folding in the context of the two main hypotheses for chaperonin function: iterative annealing and landscape modulation. We then discuss new results pointing to the importance of solvent (a previously neglected factor) in chaperonin activity. We conclude with our views on the future role of simulation in studying chaperonin activity as well as protein folding in other biologically relevant confined contexts.
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