Table 1.

Thermodynamic and spectroscopic parameters characterizing the binding of the E. coli PriB protein to etheuoderivatives of ssDNA oligomers in buffer C (pH 7.0, 10°C)^*

	14-mer	16-mer	18-mer	20-mer	24-mer	26-mer	30-mer	35-mer
	dεA(pεA)13	dεA(pεA)15	dεA(pεA)17	dεA(pεA)19	dεA(pεA)23	dεA(pεA)25	dεA(pεA)29	dεA(pεA)34
Stoichiometry	1 ± 0.1	1 ± 0.1	1 ± 0.1	1 ± 0.1	2 ± 0.2	2 ± 0.2	2 ± 0.2	2 ± 0.2
Site-size p	12	12	12	12	12	12	12	12
KN (M−1)	(5.2 ± 0.7) × 105	(9.0 ± 1.3) × 105	(1.3 ± 0.2) × 106	(1.7 ± 0.2) × 106	-	-	-	-
Ki (M−1)	(1.7 ± 0.2) × 105	(1.8 ± 0.3) × 105	(1.9 ± 0.3) × 105	(1.9 ± 0.3) × 105	(2.5 ± 0.4) × 105	(2.8 ± 0.5) × 105	(2.8 ±0.5) × 105	(1.5 ±0.3) × 105
ω	-	-	-	-	50 ± 10	45 ± 10	45 ± 10	45 ± 10
ΔF1	-	-	-	-	0.90 ± 0.03	0.80 ± 0.03	0.70 ± 0.03	0.9 ± 0.03
ΔFmax	0.77 ± 0.03	1.04 ± 0.03	1.19 ± 0.03	1.18 ± 0.03	1.32 ± 0.2	1.14 ± 0.03	1.22 ± 0.03	2.0 ± 0.05

^*The errors are standard deviations determined using 3–4 independent titration experiments.