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Updated: Jul 10, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
Published on: October 23, 2016
Chaperonin GroEL: structure and reaction cycle
K Ananda Krishna1, G Venkateswara Rao, K R S Sambasiva Rao
1Center for Biotechnology, Acharya Nagarjuna University, Guntur 522 510, Andhra Pradesh, India.
Abstract:
The structure of Escherichia coli chaperonin GroEL was studied using various experimental tools. Such studies produced information about its structure with increasing details. Moreover, remarkable advances in experimental methods provided a step forward in understanding the reaction cycle involved in GroEL-mediated protein folding. In the current review we summarize recent progress, focus on the structure of GroEL and understand the mechanism involved in GroEL-mediated protein folding. This review is divided into the following sections: (i) Section 1 provides basic understanding on protein folding, (ii) Section 2 not only describes various tools used to elucidate the structural aspects of GroEL but also provides details about its structure with particular emphasis, (iii) Section 3 describes allosteric transitions and the reaction cycle involved in GroEL-mediated protein folding, (iv) Section 4 explains iterative annealing and smoothing of the energy landscape model and finally (v) Section 5 discusses applications and recent progress.
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