Thermal stability and thermodynamic parameters of PAD4 wild-type and mutant enzymes during urea-induced denaturation.

the data were derived from Figure 3, which were monitored using circular dichroism spectrometry.
b(−), without Ca2+; (+) with 10 mM Ca2+.
cthe data were derived from the fitting results of Figure 2B and left panels of Figures 4 and 5, which were monitored using the averaged emission wavelength of fluorescence spectrometry.
dthe data were derived from the fitting results of Figure 2C and right panels of Figures 4 and 5, which were monitored using the integrated area of fluorescence spectrometry.