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. 2009 Feb 18;96(4):1495–1507. doi: 10.1016/j.bpj.2008.10.060

Table 1.

Thermodynamic parameters for the temperature-induced denaturation of CaM proteins as determined by DSC

N-domain
C-domain
Protein Tm (°C) ΔHd (kJ/mol) Tm (°C) ΔHd (kJ/mol)
apo-wt-CaM 59.5 ± 0.1 177 ± 3.2 48.3 ± 0.2 84 ± 3.2
apo-SeMet-CaM 66.2 ± 0.1 169 ± 2.7 54.7 ± 0.1 102 ± 2.7
apo-Eth-CaM 64.3 ± 0.3 142 ± 6.2 52.7 ± 0.3 103 ± 6.2
apo-Nle-CaM 57.5 ± 0.4 160 ± 20 74.6 ± 0.9 86 ± 9
apo-CT-CaM 54.7 ± 0.1 173 ± 2.2 67.1 ± 0.1 124 ± 2.2
apo-SeMet-CT-CaM 59.9 ± 0.1 166 ± 4.4 69.2 ± 0.1 123 ± 4.4
Ca2+-wt-CaM 113 ± 1.0 93 ± 1.0
Ca2+-SeMet-CaM 118 ± 1.0 97 ± 1.0
Ca2+-Eth-CaM 121 ± 1.0 100 ± 1.0
Ca2+-Nle-CaM >125 ± 1.0 97 ± 1.0
Ca2+-CT-CaM 124 ± 1.0 85 ± 1.0
Ca2+-SeMet-CT-CaM >125 ± 1.0 92 ± 1.0

Tm is the transition midpoint temperature.

ΔHd is the calorimetric enthalpy of denaturation.

Values represent the average and standard deviation (SD) of four independent measurements. All other Ka error estimates are derived from curve-fitting uncertainties.