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Chaperonin: Co-chaperonin Interactions
2014Co-chaperonins function together with chaperonins to mediate ATP-dependent protein folding in a variety of cellular compartments. Chaperonins are evolutionarily conserved and form two distinct classes, namely, group I and group II chaperonins. GroEL and its co-chaperonin GroES form part of group I and are the archetypal members of this family of ...
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The chaperonin folding machine
Trends in Biochemical Sciences, 2002Chaperonins are versatile molecular machines that assist the folding of a wide range of substrate proteins. They harness an ATPase cycle to control access of non-native proteins to hydrophobic binding sites. ATP binding promotes large conformational changes that partially bury the hydrophobic sites and initiate the binding of a co-chaperonin, creating ...
Helen R, Saibil, Neil A, Ranson
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Chaperonin-Mediated Protein Folding
Annual Review of Biophysics and Biomolecular Structure, 2001▪ Abstract  Molecular chaperones are required to assist folding of a subset of proteins in Escherichia coli. We describe a conceptual framework for understanding how the GroEL-GroES system assists misfolded proteins to reach their native states. The architecture of GroEL consists of double toroids stacked back-to-back.
D, Thirumalai, G H, Lorimer
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Allosteric regulation of chaperonins
Current Opinion in Structural Biology, 2005Chaperonins are molecular machines that facilitate protein folding by undergoing energy (ATP)-dependent movements that are coordinated in time and space by complex allosteric regulation. Recently, progress has been made in describing the various functional (allosteric) states of these machines, the pathways by which they interconvert, and the coupling ...
Horovitz, A, Willison, KR
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Assembly of Chaperonin Complexes
Molecular Biotechnology, 2001Chaperonins are a subclass of molecular chaperones that assist both the folding of newly synthesized proteins and the maintenance of proteins in a folded state during periods of stress. The best studied members of this family are the type I chaperonins, occurring in bacteria and evolutionarily derived organelles.
A R, Kusmierczyk, J, Martin
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Review: Allostery in Chaperonins
Journal of Structural Biology, 2001Chaperonins mediate protein folding in an ATP-dependent manner. ATP binding and hydrolysis by chaperonins are subject to both homotropic and heterotropic allosteric regulation. In the case of GroEL and CCT, homotropic regulation by ATP is manifested in nested cooperativity, which involves positive intra-ring cooperativity and negative inter-ring ...
A, Horovitz +3 more
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Inside the chaperonin toolbox: theoretical and computational models for chaperonin mechanism
Physical Biology, 2009Despite their immense importance to cellular function, the precise mechanism by which chaperonins aid in the folding of other proteins remains unknown. Experimental evidence seems to imply that there is some diversity in how chaperonins interact with their substrates and this has led to a number of different models for chaperonin mechanism ...
Del, Lucent +2 more
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On the oligomeric state of chloroplast chaperonin 10 and chaperonin 20
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003Type I chaperonins are fundamental protein folding machineries that function in eubacteria, mitochondria and chloroplasts. Eubacteria and mitochondria contain chaperonin systems comprised of homo-oligomeric chaperonin 60 tetradecamers and co-chaperonin 10 heptamers.
Rajach, Sharkia +7 more
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