title: Chaperonin GroEL: structure and reaction cycle.
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.
authors.affiliation: Center for Biotechnology, Acharya Nagarjuna University, Guntur 522 510, Andhra Pradesh, India.
authors.forename: K Ananda
authors.initials: KA
authors.lastname: Krishna
authors.forename: G Venkateswara
authors.initials: GV
authors.lastname: Rao
authors.forename: K R S Sambasiva
authors.initials: KR
authors.lastname: Rao
mesh_terms: D000494:Allosteric Regulation; D018834:Chaperonin 60 / Q000737:chemistry* / Q000378:metabolism; D018833:Chaperonins / Q000737:chemistry / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D008956:Models, Chemical; D008958:Models, Molecular; D017510:Protein Folding
chemical_list: D018834:Chaperonin 60; D029968:Escherichia coli Proteins; D018833:Chaperonins