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![[Figure 3]](ud5056fig3mag.jpg)
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Figure 3
Kinetic unfolding and refolding of LtPHBase. (a) Fluorescence-monitored refolding of LtPHBase after the rapid mixing of the enzyme in 7.0 M GdHCl/reaction buffer with a tenfold excess of reaction buffer. (b) The gray lines in (a) and (b) are the fit to the kinetic data (in black). Each experimental curve is the average of 50 separate traces. The inset to both curves shows a single exponential fit of the kinetic data. The residuals are based on voltage differences between the fitted and observed data. (c) The GdHCl dependence of the natural logarithm of the observed refolding and unfolding rate constants. Each experimental point was determined as the average kobs calculated from 50 independent kinetic traces. The fit of the experimental data to equation (5) ![[link]](../../../../../../logos/arrows/d_arr.gif){kind=small} is represented by a gray line. |
![[Figure 3]](ud5056fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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