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• W1969930836 abstract "▪ 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. However, most of the fundamentals of the GroEL action can be described in terms of the single ring. A key idea in our framework is that, with coordinated ATP hydrolysis and GroES binding, GroEL participates actively by repeatedly unfolding the substrate protein (SP), provided that it is trapped in one of the misfolded states. We conjecture that the unfolding of SP becomes possible because a stretching force is transmitted to the SP when the GroEL particle undergoes allosteric transitions. Force-induced unfolding of the SP puts it on a higher free-energy point in the multidimensional energy landscape from which the SP can either reach the native conformation with some probability or be trappe..." @default.
• W1969930836 created "2016-06-24" @default.
• W1969930836 creator A5036725653 @default.
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• W1969930836 date "2004-03-01" @default.
• W1969930836 modified "2023-10-16" @default.
• W1969930836 title "CHAPERONIN-MEDIATED PROTEIN FOLDING" @default.
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• W1969930836 doi "https://doi.org/10.1142/9789812703057_0012" @default.
• W1969930836 hasPublicationYear "2004" @default.
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