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• W2034351413 abstract "Chaperonins are oligomeric proteins that help other proteins fold. They act, according to the Anfinsen cage or box of infinite dilution model, to provide private space, protected from aggregation, where a protein can fold. Recent evidence indicates, however, that proteins are often ejected from the GroEL chaperonin in nonnative conformations, and repeated cycles of binding and ejection are needed for successful folding. Some experimental evidence suggests that GroEL chaperonins can act as folding catalysts in an ATP-dependent manner even when no aggregation takes place. This implies that chaperonins must somehow recognize the kinetically trapped intermediate states of a protein. A central puzzle is how a chaperonin can catalyze the folding reaction of a broad spectrum of different proteins. We propose a physical mechanism by which chaperonins can flatten the energy barriers to folding in a nonspecific way. Using a lattice model, we illustrate how a chaperonin could provide a sticky surface that helps pull apart an incorrectly folded protein so it can try again to fold. Depending on the relative sizes of the protein and the chaperonin cavity, folding can proceed both inside and outside the chaperonin. Consistent with experiments, we find that the folding rate and amount of native protein can be considerably enhanced, or sometimes reduced, depending on the amino acid sequence, the chaperonin size, and the binding and ejection rates from the chaperonin." @default.
• W2034351413 created "2016-06-24" @default.
• W2034351413 creator A5013305919 @default.
• W2034351413 creator A5053481856 @default.
• W2034351413 date "1996-03-01" @default.
• W2034351413 modified "2023-10-16" @default.
• W2034351413 title "A simple model of chaperonin-mediated protein folding" @default.
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• W2034351413 doi "https://doi.org/10.1002/(sici)1097-0134(199603)24:3<345::aid-prot7>3.0.co;2-f" @default.
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