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. Author manuscript; available in PMC: 2015 Oct 14.
Published in final edited form as: Org Biomol Chem. 2014 Oct 14;12(38):7523–7536. doi: 10.1039/c4ob01456a

Table 2.

SPR analysis of kinetic rate constants and equilibrium affinities for PAs binding to their cognate site TGGAGA at 25 °C with 50 mM NaCl*. ΔTm values with cognate DNA are included for comparison.

PA Kinetics KD (nM)
ka
(×106M−1s−1)
kd
(×10−3s−1)
Kinetic fit Steady state ΔTm (°C)
KA1033 4.7 ± 0.7 12 ± 1 2.5 ± 0.4 2.8 ± 0.3 7.8
KA1011 2.6 ± 0.3 96 ± 6 36.4 ± 0.4 36.6 ± 0.1 2.0
KA1013 3.7 ± 0.4 45 ± 7 12.1 ± 0.4 10.3 ± 0.5 5.4
KA2127 1.8 ± 0.3 4.7 ± 0.3 2.6 ± 0.2 2.9 ± 0.2 8.0
KA2128 0.7 ± 0.2 13 ± 2 18.6 ± 0.8 17.5 ± 0.1 3.6
KA2129 1.1 ± 0.2 29 ± 5 26.3 ± 2.2 24.0 ± 0.5 3.2
KJK6021 1.3 ± 0.2 2.6 ± 0.2 2.0 ± 0.2 2.2 ± 0.3 8.8
*

Errors listed are the standard errors for the fits.