Table 3.
Steady-state equilibrium dissociation constants (Kd) of HgII binding to DMAT–C,DMAC–T, DMAT–T or wild-type C–T in duplex DNAa
Sequence | Temperature | K d (nM) non-specificb | K d (nM) mismatch specificc |
---|---|---|---|
X13 DMAT–C | 25°C | - | 152 ± 4 |
X13 DMAT–C | 15°C | - | 107 ± 4 |
X13 DMAT–C | 4°C | - | 56 ± 4 |
X15 DMAT–C | 25°C | 1300 ± 300 | 123 ± 76 |
X15 DMAC–T | 25°C | 2300 ± 300 | 153 ± 27 |
X15 DMAC–G, X14 C–T | 25°C | 2200 ± 400 | 107 ± 45 |
X15 DMAC–G | 25°C | 2260 ± 130 | - |
X13 DMA T–T | 25°C | - | 77 ± 4 |
X13 DMA T–T | 15°C | - | 122 ± 11 |
X13 DMA T–T | 4°C | - | 144 ± 27 |
a Reported values = mean ± standard deviation from three independent measurements. Samples contained 25 nM of DNA in an aqueous buffer containing 200 mM Na2HPO4, 100 mM citric acid and 100 mM NaNO3 (pH 7.35). Kd values were calculated by fitting quenching data to either a monoexponential curve (eq 11, SI) or to a biphasic curve (eq 12, SI). All R2 values were ≥ 0.97 (Supplementary Figures S16 and S17, SI). For duplex sequences see Supplementary Table S1, SI.
b Represents local, mismatch-independent binding to duplex DNA.
c Represents local, mismatch-dependent binding to duplex DNA.