. 2017 Nov 24;7:16321. doi: 10.1038/s41598-017-16360-y

Table 2.

Results of the global fitting of DSC thermograms for various proteins.

Protein	Model*	1st step	2nd step
Lysozyme wild type	Partially reversible three-state equilibrium (C)	T _m = 345.03 ± 0.05 K ∆H = 516 ± 3 kJ mol⁻¹ ∆C _p = 7.5 ± 0.7 kJ mol⁻¹K^−1**	E = 18 ± 1 kJ mol⁻¹ T _f = 3.2 ± 1.4 kK ∆H = −37 ± 10 kJ mol⁻¹
SpA mutant	Reversible two-state (A)^‡‡	T _m = 328.44 ± 0.07 K ∆H = 102.4 ± 0.7 kJ mol⁻¹ ∆H _vh = 169 ± 1 kJ mol⁻¹ ∆C _p = 1.38 ± 0.04 kJ mol⁻¹K⁻¹	N/A
DbjA wild type	Irreversible two-state (B)	E = 418 ± 3 kJ mol⁻¹ T _f = 337.6 ± 0.1 K ∆H = 337 ± 3 kJ mol⁻¹ ∆C _p = 5.4 ± 0.1 kJ mol⁻¹K⁻¹	N/A
LinB wild type	Irreversible two-state (B)	E = 294 ± 3 kJ mol⁻¹ T _f = 338.6 ± 0.2 K ∆H = 397 ± 5 kJ mol⁻¹ ∆C _p = 8.0 ± 0.1 kJ mol⁻¹K⁻¹	N/A
DhaA wild type	Partially reversible three-state equilibrium (C)	T _m = 323.8 ± 0.1 K ∆H = 338 ± 2 kJ mol⁻¹	E = 75 ± 13 kJ mol⁻¹ T _f = 436 ± 27 K ∆H = 70 ± 19 kJ mol^−1* ∆C _p = 10.2 ± 0.5 kJ mol⁻¹K^−1
DhaA115 mutant	General three-state (D)	E ₁ = 436.5 ± 0.1 kJ mol⁻¹ T _f1 = 358.0 ± 0.01 K E ₋₁ = 46.7 ± 0.1 kJ mol⁻¹ T _f − 1 = 689.4 ± 0.1 K ∆H = 596 ± 5 kJ mol⁻¹	E = 109.1 ± 0.1 kJ mol⁻¹ T _f = 431.6 ± 0.1 K ∆H = −160 ± 40 kJ mol^−1‡ ∆C _p = 6.1 ± 0.4 kJ mol⁻¹K^−1**

^*The model is defined for the main peak; **∆C_p is given as a combined value for two steps; N/A – not applicable. The values are given with 95% confidence intervals from the fitting; ^‡ ∆H values calculated at the apparent peak temperature and, therefore, resembling the area under the peak; the values used for modelling of ∆H(T), i.e. values of ∆H(T _f ), were 1126 ± 301 and −566 ± 40 kJ mol⁻¹ for DhaA wild type and 115, respectively; ^‡‡The reversible model was augmented by the van’t Hoff enthalpy.