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• W2000763649 startingPage "478" @default.
• W2000763649 abstract "We have studied the effect of the components of the GroE molecular chaperone machine on the refolding of the Escherichia coli enzyme β-galactosidase, a tetrameric protein whose 116-kDa protomers should not completely fit within the central cavity of the GroEL toroid. In the absence of other additives, GroEL formed a weak complex with chemically denatured β-galactosidase, reduced its propensity to aggregate, and increased the recovery yields of active enzyme twofold without altering its folding pathway. When present together with the chaperonin, ATP —and to a lesser extent AMP-PNP —reduced the recovery yields and led to the resumption of aggregation. The use of the complete chaperonin system (GroEL, GroES, and ATP) eliminated the GroEL-mediated increase in recovery and folding proceeded less efficiently than in buffer alone. This unusual behavior can be explained in terms of a chaperonin “buffering” effect and the different affinities of GroE complexes for denatured β-galactosidase." @default.
• W2000763649 created "2016-06-24" @default.
• W2000763649 creator A5011469865 @default.
• W2000763649 creator A5028122420 @default.
• W2000763649 date "1996-03-01" @default.
• W2000763649 modified "2023-10-09" @default.
• W2000763649 title "Influence of the GroE molecular chaperone machine on the in vitro refolding of<i>Escherichia coli</i>β-galactosidase" @default.
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• W2000763649 doi "https://doi.org/10.1002/pro.5560050309" @default.
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