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The observed association rate constant for the morphine binding reaction was calculated to be 215 M−1 s−1.
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The binding number of [Cu dafone)2]Br2 for each salmon sperm dsDNA chain and equilibrium constant of the binding reaction were calculated to be 3 and 2.8 × 1012 L3 mol−3, respectively.
The percentage inhibition of the reaction was calculated from a control reaction containing only vehicle.
This binding constant(s) and its corresponding molar heat enthalpy (ΔH) for the reaction are calculated directly from the plot of heat evolved for each injection (ΔQi) versus molar ratio of ligand and protein using the software associated with ITC.
The binding site number (n ≈ 1) and corresponding thermodynamic parameters (ΔG), (ΔH) and (ΔS) were calculated, indicated that binding reaction was endothermic and the hydrophobic interactions plays a major role in stabilizing the complex.
The binding reaction was stopped by washing 5 times with 150 μl of binding buffer.
According to the Förster's non-radiative energy transfer theory, the binding distance r between AMA and BSA was calculated, the result represents a static quenching, and the binding reaction is spontaneous and is largely mediated by hydrophobic forces.
The binding constant was calculated to be 4.57 × 104 M−104
Binding energy was calculated by applying CHARMm forcefield.
An average binding ratio was calculated ± one standard deviation.
The binding affinity was calculated at −8.9 kcal mol−1.
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