. Author manuscript; available in PMC: 2013 Sep 18.

Published in final edited form as: Biochemistry. 2012 Sep 6;51(37):7367–7382. doi: 10.1021/bi300956t

Table 1.

Equilibrium fluorescence anisotropy binding parameters for polymerase binding to DNA

Dpo1			Dpo4
Temp (^oC)	K_d1 (μM)^a	K_d2 (μM)^a	Temp (^oC)	K_d1 (μM)^a	K_d2 (μM)^a
6.8	0.322 ± 0.023	17.2 ± 0.3	6.8	0.435 ± 0.116	9.32 ± 0.88
12.0	0.208 ± 0.057	8.01 ± 1.21	12.0	0.329 ± 0.107	5.16 ± 0.05
17.0	0.170 ± 0.023	5.78 ± 0.13	17.0	0.214 ± 0.003	4.70 ± 1.01
22.2	0.109 ± 0.016	4.70 ± 0.78	22.1	0.176 ± 0.010	3.22 ± 0.72
27.4	0.105 ± 0.003	3.70 ± 0.32	27.3	0.164 ± 0.009	2.82 ± 0.35
32.8	0.094 ± 0.001	2.68 ± 0.11	32.9	0.130 ± 0.004	3.01 ± 0.92
38.0	0.097 ± 0.003	2.48 ± 0.06	37.8	0.140 ± 0.066	2.33 ± 0.40
43.3	0.144 ± 0.003	2.60 ± 0.22	43.2	0.133 ± 0.026	1.72 ± 0.46
48.8	0.144 ± 0.015	1.82 ± 0.36	48.8	0.125 ± 0.051	2.32 ± 0.95
53.9	0.113 ± 0.032	2.41 ± 0.79	53.8	0.155 ± 0.065	2.71 ± 0.99
58.9	0.208 ± 0.022	3.21 ± 0.21	58.9	0.444 ± 0.115	3.81 ± 0.28
63.7	0.198 ± 0.026	4.52 ± 0.40	65.2	0.674 ± 0.080	7.18 ± 0.93

K_d1 and K_d2 are the equilibrium dissociation constants for the first and second binding events, respectively. Values are means and standard errors from parameters fit to Equation 5 from at least three independent titration experiments at each temperature.