Figure 7.

Observed refolding (open symbols) and unfolding (filled symbols) relaxation times of WT (circles) and S134N (upside-down triangle) (A) $\text{mAS}-\text{SOD}{1}_{\text{Apo}}^{2\text{SH}}$ and (B) $\text{mAS}-\text{SOD}{1}_{\text{Zn}}^{2\text{SH}}$ monitored by CD at 230 nm, at pH 7.2 and 20 °C, and plotted as a function of final denaturant concentration. The data are shown with the best fit line to a two-state folding reaction for WT(solid line) and S134N (dashed line). The protein and Zn concentrations were 10 μM and the buffer used was 20 mM HEPES, 1 mM TCEP pH 7.2.