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. 2015 Jun 24;6(10):5578–5585. doi: 10.1039/c5sc01381j

Table 3. The binding thermodynamic parameters of different cofactors (CuLn) to human telomeric G-quadruplex DNA in 30 mM NH4Cl at 298 K.

Cofactor High-affinity binding site
Low-affinity binding site
K a1/M–1 n 1 ΔH1 a TΔS1 a ΔG1 a K a2/M–1 n 2 ΔH2 a TΔS2 a ΔG2 a
CuL1 b (1.7 ± 0.2) × 107 1.0 4.4 ± 0.1 –14.3 –9.9 (6.6 ± 0.5) × 105 5.0 –2.2 ± 0.1 –5.7 –7.9
CuL2 b (1.7 ± 0.3) × 107 1.1 4.2 ± 0.3 –14.0 –9.8 (1.0 ± 0.1) × 106 5.8 –2.1 ± 0.1 –6.1 –8.2
CuL3 b (1.7 ± 0.3) × 107 1.1 6.7 ± 0.2 –16.6 –9.9 (1.1 ± 0.1) × 106 6.8 –1.5 ± 0.1 –6.8 –8.3
CuL4 b (1.7 ± 0.3) × 107 1.2 4.2 ± 0.1 –14.1 –9.9 (5.8 ± 0.6) × 105 5.4 –2.5 ± 0.1 –5.3 –7.8
CuL5 c (2.0 ± 0.5) × 105 2.5 –1.1 ± 0.1 –6.1 –7.2
CuL6 d

aUnits are kcal mol–1.

bThe data were obtained by the two-event binding model.

cThe data were obtained by the one-event binding model.

dThe affinity between the reactants is too low, neither the affinity nor the enthalpy of binding can be reliably determined.