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. Author manuscript; available in PMC: 2011 Nov 30.
Published in final edited form as: J Mol Biol. 2010 Feb 12;398(1):8–25. doi: 10.1016/j.jmb.2010.02.009

Table 2.

Macroscopic and intrinsic binding constants, K20 and Kin, and the site-size, n, characterizing the binding of the PriB protein to different ssDNA homo-oligomers, dN(pN)19, in buffer C (pH 7.0, 10 °C). The values of K20 for the unmodified 20-mers have been determined using the MCT Method (details in text).*

dεA(pεA)19 dA(pA)19 dT(pT)19 dC(pC)19
K20 (M−1) (1.7 ± 0.4) × 106 (3.5 ± 0.8) × 105 (3.0 ± 0.7) × 108 (2.5 ± 0.4) × 107
Kin (M−1) (1.9 ± 0.5) × 105 (3.9 ± 0.8) × 104 (3.3 ± 0.7) × 107 (2.8 ± 0.4) × 106
n 12 12 12 12
*

Errors are standard deviations determined using 3–4 independent titration experiments.