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Isothermal titration calorimetry experiments were used to acquire binding constants for the inhibitor MP265 and nucleotides that bind to the active site of ΔCcMreBdh.
Equilibrium binding constants for the axial coordination of inorganic anions were determined by cyclic voltammetry measurements.
In this model, the determined binding affinity constants become intrinsic binding constants for the individual EF-hands.
A strong NADH binding in contrast to weaker NAD+ binding of the protein was inferred from fluorometrically determined binding constants for the dinucleotide cofactor.
Extraction of microscopic binding constants for the linked equilibrium between anion and proton binding indicates that anion selectivity by YFP is related to hydration forces.
Parameters, such as the diffusion coefficient of NR, binding site size in base pairs and the ratio of the binding constants for the oxidized and reduced forms of the bound species were obtained.
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The binding constant for the interaction with HVR1 was 1.39 nM for Fab 30F1 and 3.96 nM for Fab 30F3.
The binding properties of the investigated ruthenium complex to human serum albumin have been studied and the apparent binding constant for the formation of the protein-ruthenium adduct was determined to be 1.1 × 105 M− 1.
The binding constant for the interaction of Cu II) ion with the present unsubstituted quinone is found to be relatively higher than that with quinones containing electron withdrawing chlorine atom and electron releasing methyl group reported in literature.
All the obtained compounds have been tested for their in vitro cytotoxic activity and the most potent of them showed an IC50 of 9 μM upon the human lung cancer (A-549) cell and a binding constant, for the intercalation with calf thymus DNA, of 9.6 × 104 M−104
We measured the affinities of wild type activin A, chimera mutant βAext+/βAext+ and deletion mutant βAWHD/βAWHD for ActRIIB directly using a competition binding analysis, which revealed a weaker binding constant for the N-terminal insertion mutant and wrist helix deletion mutant (βAext+/βAext+ IC50 = 5.99 nM; βAWHD/βAWHD IC50 = 47.6 nM; human activin A IC50 = 4.14 nM) (Figs. 4A and S7A).
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