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- W2032911145 abstract "We propose protein PTB1∶4W as a good candidate for engineering into a downhill folder. PTB1∶4W has a probe-dependent thermal unfolding curve and sub-millisecond T-jump relaxation kinetics on more than one time scale. Its refolding rate in denaturant is a non-linear function of denaturant concentration (curved chevron plot). Yet at high denaturant concentration its unfolding is probe-independent, and the folding kinetics can be fitted to a single exponential decay. The domain appears to fold via a mechanism between downhill folding and activated folding over several small barriers, and when denaturant is added, one of these barriers greatly increases and simplifies the observed folding to apparent two-state kinetics. We predict the simplest free energy function consistent with the thermal denaturation and kinetics experiments by using the singular value Smoluchowski dynamics (SVSD) model. PTB1∶4W is a natural ‘missing link’ between downhill and activated folding. We suggest mutations that could move the protein into the downhill folding limit." @default.
- W2032911145 created "2016-06-24" @default.
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- W2032911145 date "2010-01-01" @default.
- W2032911145 modified "2023-10-07" @default.
- W2032911145 title "A natural missing link between activated and downhill protein folding scenarios" @default.
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- W2032911145 doi "https://doi.org/10.1039/b925033f" @default.
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