Sentence examples for binding was calculated to from inspiring English sources
Using PyMOL, ΔSASA of ASB9 EloBC and Cul5NTD binding was calculated to be −1238 Å, of which 437 Å is due to the burial of polar atoms and 801 Å from the burial of hydrophobic regions.
With an enthalpy (Δ H°) of 6.00 ± 0.09 kcal/mol and an association constant (Ka) of (1.79 ± 0.20) × 10 M–1 for CaM Fas DD binding, the entropy (− TΔ S°) for CaM Fas DD binding was calculated to be −14.87 ± 0.12 kcal/mol and the Gibbs free energy (Δ G°) for CaM Fas DD binding to be −8.87 ± 0.07 kcal/mol.
The binding constant was calculated to be 4.57 × 104 M−104
The observed association rate constant for the morphine binding reaction was calculated to be 215 M−1 s−1.
Moreover, the stoichiometry of the C4D-NADH complex formed was found to be 1 1 and the binding constant was calculated to be 3.74 × 105 M−105
The binding constant was calculated to be 1.909 × 103 L mol−1 at 288 K and it decreased with the increase of the temperature.
For the 25TAC inhibitor, the number of binding sites was calculated to be 36 [2 × (25 – 8 + 1) = 36].
The binding capacity was calculated to be 0.8 ± 0.1 μM/g, which was in the range for CBD-fusion proteins [ 21- 23].
For L2S, the binding event was calculated to have an association constant Ka of 1.45 × 10 M–1 and a stoichiometry of 2.0; for L1L2S, a Ka of 1.32 × 10 M–1 with a stoichiometry of 0.83 was found, while the absence of quantifiable heat changes with L3S′ suggests an only modest strength of binding of L3S′ to PDK2.
The ITC data revealed that the interaction of Dat with dopamine appeared to be an exothermic reaction with enthalpy (Δ H =−7.85 kcal/mol, and entropy (Δ S =−5.32 cal/mol per K. Fitting to one set of the site-binding model, the Ka of dopamine binding to Dat was calculated to be 3.88×10 M−1, and the binding constant Kd was 25.9 μM.
