Post-translational S-Nitrosylation Is an Endogenous Factor Fine Tuning the Properties of Human S100A1 Protein

TABLE 2

Thermodynamic parameters for calcium binding estimated from isothermal titration of protein solution with CaCl2

For both forms of S100A1, in accordance with stoichiometry derived from Job plots, sequential binding of Ca2+ by two binding sites is followed by binding to another two cations by yet unidentified site(s).

Site n K ΔG ΔH ΔS
kcal/mol kcal/mol cal/mol/K
apo-S100A1
    1 1 2.4 ± 0.8 103 m−1 −4.6 ± 0.1 2.9 ± 0.4 25.3
    2 1 1.8 ± 0.2 103 m−1 −4.5 ± 0.1 −6.0 ± 1.5 −5.1
    3 2 6.0 ± 1.2 103 m−1 −5.2 ± 0.2 6.5 ± 1.8 39.2
apo-S100A1-NO
    1 1 3.1 ± 0.5 107 m−2 −10.3 ± 0.1 4.5 ± 0.3 49.6
    2 1
    3 2 1.8 ± 0.3 103 m−1 −4.5 ± 0.2 1.1 ± 0.2 18.7

This Article

  1. JBC vol. 287 no. 48 40457-40470