Table 1.

Summary of dissociation constants obtained from FP binding assays^a,b.

	Gq23	Comp	polyA	polyG
	K d (μM)	K d (μM)	K d (μM)	K d (μM)
RPA
NaCl (mM)
100	0.05	0.07	0.07	0.26±0.06
500	0.04 ± 0.02	0.06 ± 0.01	0.17 ± 0.02	nd
1250	0.37 ± 0.08	0.07	nd	nd
1500	0.85 ± 0.16	0.07	nd	nd
RPA-AB
NaCl (mM)
100	0.44 ± 0.06	0.66 ± 0.21	1.83 ± 0.39	1.54 ± 0.35
500	3.28 ± 0.68	1.79 ± 0.36	nd	nd
1250	nd	2.65 ± 0.15	nd	nd
1500	nd	2.45 ± 0.33	nd	nd
RPA-CDE-core
NaCl (mM)
10	0.16 ± 0.05	0.22 ± 0.01	0.53 ± 0.03	1.72 ± 0.13
100	0.55 ± 0.09	0.42 ± 0.04	5.88 ± 0.72	11.01 ± 0.97
500	11.92 ± 0.12	0.75 ± 0.02	nd	nd
1250	nd	2.81 ± 0.16	nd	nd
RPA-DE
NaCl (mM)
10	6.68 ± 0.23	nd	nd	4.30 ± 0.20
100	nd	nd	nd	19.18 ± 3.68
RPA-C
NaCl (mM)
10	3.62 ± 0.26	3.32 ± 0.02	nd	1.18 ± 0.18
100	nd	nd	nd	nd

^aValues reported here are averages from two separate experiments where each data point was performed in triplicate. Error values obtained were between 5 and 10%.

^bData collected under stoichiometric conditions is underlined and the K _d is underestimated.

nd = not determinable (the experiments were performed but binding was not detectable). The K _ds cannot be estimated because at higher protein concentrations no binding is detected, and binding saturation is not obtained.