Results 211 to 220 of about 34,485 (247)

Origin of chaperone dependence and assembly complexity in Rubisco’s biogenesis

Ng JZY, Wiens D, Schulz L, Hergenröder A, Küffner AM, Geil C, Erb TJ, Hochberg GKA.   +7 more
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Purification of chaperonins

Journal of Chromatography B: Biomedical Sciences and Applications, 1999
The availability of protein samples of sufficient quality and in sufficient quantity is a driving force in biology and biotechnology. Protein samples that are free of critical contaminants are required for specific assays. Large amounts of highly homogeneous and reproducible material are needed for crystallography and nuclear magnetic resonance studies
E, Quaite-Randall, A, Joachimiak
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Chaperonin: Co-chaperonin Interactions

2014
Co-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, 2002
Chaperonins 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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Chaperonins

2012
on line http://www.els ...
CHIARALUCE, Roberta, CONSALVI, Valerio
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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, 2005
Chaperonins 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, 2001
Chaperonins 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, 2001
Chaperonins 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, Y, Fridmann, G, Kafri, O, Yifrach   +3 more
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