. 2001 Sep;10(9):1758–1768. doi: 10.1110/ps.11601

Table 3.

Thermal denaturation properties of Apo PCaM1–75

Protein	T_m (°C)^a	ΔH°_VH (kcal/mole)^a	ΔCp (cal/K•mole)^a
WT	58.9 ± 0.4	51.3 ± 0.8	1121 ± 360
V35I/D50N	58.9 ± 0.3	50.0 ± 1.0	1057 ± 450
G40E	41.8 ± 0.7	38.4 ± 1.9	867 ± 442
G40E,D50N	40.8 ± 0.5	34.9 ± 2.1	879 ± 360
D50G	53.9 ± 0.1	49.4 ± 0.8	1360 ± 60
E54K	61.2 ± 0.3	46.3 ± 3.2	1033 ± 90
G59S	52.8 ± 0.2	48.4 ± 0.4	1403 ± 90

Thermal unfolding studies were performed as described in Materials and Methods. Data were fit to a two-state model of unfolding described by equation 5.

^a Average values and standard deviations from three trials are reported. The √var for fits of each individual trial ranged from 0.003–0.008 with an average of 0.004.