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• W2002938172 abstract "The β2 subunit of Escherichia coli tryptophan synthase can be either unfolded in 6 M guanidine, or extensively denatured at acidic pH. These two denatured form of β2 have different circular dichroism spectra and thus correspond to distinct physical states. Here we compare the folding pathways of these two different denatured forms of β chains. We describe the kinetics of regain of a variety of physical, functional, ad immunochemical signals characteristic of six successive steps previously identified on the folding pathway of guanidine unfolded β2. It is shown that whereas identical molecular events over with the same kinetics, the two folding pathways are different, and involve different structural intermediates." @default.
• W2002938172 created "2016-06-24" @default.
• W2002938172 creator A5000077022 @default.
• W2002938172 creator A5026060301 @default.
• W2002938172 date "1989-01-01" @default.
• W2002938172 modified "2023-09-23" @default.
• W2002938172 title "Alternate succession of steps can lead to the folding of a multidomain oligomeric protein" @default.
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• W2002938172 doi "https://doi.org/10.1002/prot.340060406" @default.
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