Table 2 Energetic parameters for the denaturation of hPGK1 variants determined from DSC data in the absence or the presence of urea.

From: Loss of stability and unfolding cooperativity in hPGK1 upon gradual structural perturbation of its N-terminal domain hydrophobic core

Variant

Urea (M)

Tm (°C )

ΔH (kcal·mol−1)

Ea (kcal·mol−1)

WT

0

53.5 ± 0.7

162 ± 10

168 ± 15

0.5

51.2 ± 0.7

142 ± 12

140 ± 7

1

48.7 ± 0.9

136 ± 13

115 ± 4

F25L

0

51.6 ± 0.6

156 ± 6

150 ± 12

0.5

49.2 ± 0.7

133 ± 6

129 ± 4

1

46.4 ± 0.9

126 ± 16

105 ± 1

F25V

0

50.4 ± 0.7

153 ± 11

140 ± 12

0.5

47.5 ± 0.9

133 ± 14

106 ± 5

1.1

44.3 ± 1.3

114 ± 22

80 ± 2

F25A

0

48.9 ± 0.8

153 ± 14

119 ± 9

0.5

45.8 ± 1.1

124 ± 16

89 ± 3

1

42.8 ± 1.7

109 ± 18

68 ± 3

F25G

0

46.7 ± 0.9

155 ± 15

94 ± 3

0.5

43.5 ± 1.6

123 ± 11

71 ± 4

1

41.1 ± 1.9

108 ± 19

59 ± 5

F25W

0

49.2 ± 0.7

140 ± 17

120 ± 6

0.5

46.3 ± 0.9

120 ± 18

93 ± 2

1

43.0 ± 1.5

96 ± 16

72 ± 5

  1. Data are the mean ± s.d. for three different scan rates (4, 2.5 and 1 °C min−1) at 7–15 µM protein concentration and using a two-state irreversible model.
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