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Stern Volmer analysis showed the binding stoichiometry to be 1 1 (host guest) and a binding constant of 1.6 × 104 M−1, calculated using the Benesi Hilderbrand equation.
Stern Volmer analysis showed the binding stoichiometry to be 1 2 (host-guest) with a binding constant of 1.8×1010 M−2, calculated using the Benesi Hilderbrand equation.
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The binding stoichiometry was determined to be 0.86, indicating that (1) each ssDNA molecule may provide a single binding site for the oxidized SOD1, and (2) the oxidized SOD1 proteins bound to the ssDNA may not aggregate.
Again the binding stoichiometry (n) was determined to be ∼1 in both cases (Fig. 2), confirming that a specific 1∶1 complex is formed in each case.
The binding stoichiometry from ITC is clearly 1∶1, but it should be noted that a 2∶2 complex is by no means excluded by this result, since such details are indistinguishable in this experiment.
The binding stoichiometry was consistent with the fact that 20 cysteine residues are contained in mammalian metallothioneins and maximally six iAsIII can bind to the protein.
To confirm that this phase is associated with a single nucleotide site, its PAPS binding stoichiometry was determined.
The methods of data analysis to derive the equilibrium constant and binding stoichiometry are also discussed in the chapter.
Nevertheless, the result is consistent with the idea that the AtCaM6 W980 binding stoichiometry is 2 1.
The binding stoichiometry was determined at peptide concentrations between 1 µM and 10 µM, while the binding constants were determined at a peptide concentration of 1 µM.
But, higher binding stoichiometry was also abundant in the cells expressing both eGFP-CaM and the nonlabeled form of αCaMKII, presumably because αCaMKII is binding to multiple copies of eGFP-CaM.
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