Chaperonin GroEL: Structure and Reaction Cycle

Author(s): K. Ananda Krishna, G. Venkateswara Rao, K. R.S. Sambasiva Rao

Journal Name: Current Protein & Peptide Science

Volume 8 , Issue 5 , 2007

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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.

Keywords: Chaperonin, Escherichia coli, iterative annealing, molecular chaperonins, GroEL, GroES, protein folding

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Article Details

Year: 2007
Page: [418 - 425]
Pages: 8
DOI: 10.2174/138920307782411455
Price: $65

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