. 2005 Jan 7;385(Pt 2):363–370. doi: 10.1042/BJ20041153

Table 2. Binding of Ac-LRTQpNA and Ac-ELRTQpNA to HAV 3C.

Association rate constants k_on, dissociation rate constants k_off and dissociation constants K_D were obtained from SPR experiments. For the kinetic analysis a Langmuir 1:1 binding model with corrections for a drifting baseline and mass transfer was applied using global fitting (experiments A and B) [35]. Analyte concentrations were: experiment A, 25, 50, 100, 250, 500, 1000 and 2000 μM; experiment B, 25, 50, 100, 250, 500, 2000 and 4000 μM. Data in experiments C and D resulted from an equilibrium analysis. The analyte concentrations were: *25, 50, 100, 250, 500, 2000, 4000, 6000 μM; †25, 50, 100, 250, 500, 2000 μM; ‡25, 50, 100, 250, 500, 2000, 4000, 8000 μM. 3000 to 4000 RU of ligand were immobilized in all cases. wt, wild-type.

Analyte	Experiment	Ligand	k_on (M⁻¹·s⁻¹)	k_off (s⁻¹)	K_D×10⁻³ (M⁻¹)	χ²
Ac-LRTQ-pNA	A
		wt	132	0.181	1.4	1.2
		C24S	213	0.243	1.1	1.1
		C24S/C172A	187	0.041	0.2	1.4
Ac-ELRTQ-pNA	B
		wt	35	0.014	0.4	2.8
		C24S	18	0.035	1.9	2.8
		C24S/C172A	37	0.015	0.4	2.7
Ac-LRTQ-pNA	C
		wt*			5.0	11
		wt†			1.8	3
		C24S*			3.9	7
		C24S†			1.8	2
		C24S/C172A*			6.4	11
		C24S/C172A†			2.6	5
Ac-ELRTQ-pNA	D
		wt‡			2.8	28
		wt†			1.3	11
		C24S‡			4.3	54
		C24S†			1.0	18
		C24S/C172A‡			5.7	136
		C24S/C172A†			0.5	30