Table 3.

Kinetic rate constants, activation energies and thermodynamic parameters for FPR binding.

	koff (s−1)	kon (μM−1 s−1)	Eoff (kcal/mol)	Eon (kcal/mol)	kd (μM)	ΔG (kcal/mol)	ΔH (kcal/mol)	ΔS (cal/mol/K)
Pre2	46 ± 4	0.46 ± 0.05	17 ± 1	8.6 ± 0.5	100 ± 10	−5.3 ± 0.2	−8.4 ± 0.5	−11 ± 1
I16T	29 ± 3	0.73 ± 0.07	23 ± 1	3.0 ± 0.2	40 ± 4	−5.8 ± 0.2	−17 ± 1	−39 ± 3
D194A	7.8 ± 0.6	1.6 ± 0.1	13 ± 1	8.9 ± 0.4	4.9 ± 0.5	−7.0 ± 0.3	−4.1 ± 0.2	+10 ± 1
wt	0.6 ± 0.1	2.6 ± 0.3	—	—	0.23 ± 0.02	−8.8 ± 0.3	—	—

Experimental conditions are: 400 mM ChCl, 50 mM Tris, 0.1% PEG8000, pH 8.0. Values of rate constants are at the reference temperature T₀ = 288.15 K (15 °C). Definitions are: $K_d=\frac{k_{off}}{k_{on}}$ (equilibrium dissociation constant); ΔG = RTlnK_d (binding free energy); ΔH = E_on − E_off (binding enthalpy); $\mathrm{\Delta }S=\frac{\mathrm{\Delta }H-\mathrm{\Delta }G}{T}$ (binding entropy). Values for wild-type are from previously published work⁸.