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pubmed-article:10339536pubmed:abstractTextHighly nonexponential folding kinetics in aqueous solution have been observed during temperature jump-induced refolding of two proteins, yeast phosphoglycerate kinase and a ubiquitin mutant. The observations are most easily interpreted in terms of downhill folding, which posits a heterogeneous ensemble of structures en route to the folded state. The data are also reconciled with exponential kinetics measured under different experimental conditions and with titration experiments indicating cooperative folding.lld:pubmed
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pubmed-article:10339536pubmed:articleTitleObservation of strange kinetics in protein folding.lld:pubmed
pubmed-article:10339536pubmed:affiliationSchool of Chemical Sciences and Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana, IL 61801, USA.lld:pubmed
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