Observation of strange kinetics in protein folding.
Highly 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.
Sabelko
J
J
School of Chemical Sciences and Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana, IL 61801, USA.
Ervin
J
J
Gruebele
M
M
D019943:Amino Acid Substitution; D006801:Humans; D007700:Kinetics; D019906:Nuclear Magnetic Resonance, Biomolecular; D010735:Phosphoglycerate Kinase / Q000737:chemistry* / Q000378:metabolism*; D017354:Point Mutation; D011489:Protein Denaturation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics; D014452:Ubiquitins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D011994:Recombinant Proteins; D014452:Ubiquitins; D010735:Phosphoglycerate Kinase