Table 2. Thermodynamic parameters for the unfolding of T. aquaticus SCS.

Protein	† (kJmol1)	m † (kJmol1 M 1)	Correlation coefficient†	[GdmCl]1/2 ‡ (M)
Whole enzyme
First transition	29 4	13 2	0.986	2.2
Second transition	25 1	7.1 0.4	0.998	3.7
-Subunit	6.7 0.4	3.1 0.2	0.998	2.2
-Subunit	10.0 0.8	5.4 0.4	0.997	2.0

^†These values were calculated by extrapolation of a replot of the molar ellipticities using the equation G = RTlnK, where K = (_{N obs})/(_{obs U}), _N is the molar ellipticity observed at 0M GdmCl, _U is the molar ellipticity observed at the maximum concentration of GdmCl and _obs is the observed molar ellipticity. In the vicinity of the transition the resulting plot was fitted to the equation G = m[GdmCl] (for a review, see Myers et al., 1995 ▶) with the correlation coefficient listed.

^‡These values were obtained by interpolation from the graphs and are consistent with the values obtained by the calculation [GdmCl]_1/2 = [/m.