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. 2002 May;11(5):1091–1100. doi: 10.1110/ps.4970102

Table 2.

Comparison of the thermodynamic parameters of the interaction of E3 and E1 with the PSBD of E2

Enzyme Kaa (M−1) ΔG°b (kcal/mol) ΔH°c (kcal/mol) TΔS°d (kcal/mol) ΔCpc (kcal/molK) Protons linkedc (n)
E3 1.7 × 109 −12.6 +2.2 +14.8 −316 −0.02
E1 3.1 × 109 −12.9 −8.4 +4.5 −470 +0.11

All the kinetic and thermodynamic parameters are taken from experiments in HBS buffer, pH 7.4 at 25°C.

a Obtained from SPR analysis.

b Calculated from ΔG° = −RT lnKa.

c Calculated from ITC measurments.

d Calculated from TΔS° = ΔH° − ΔG°.