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The quenching constants and binding constants were determined for pSCX4 FL and pSCX4-FL Cu2+ systems.
Apparent binding constants were determined and ranged between 1.22 and 23.96 μM−1.
Composition of the complexes formed was determined from mass spectrometry and the binding constants were determined from fluorescence titration data.
The stoichiometry of the H-bonded complexes is found to be 1 1 (receptor cyanide) and the binding constants are determined to be in the order of 105 M−105
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.
Kinetic binding constants were determined by surface plasmon resonance using a BIACORE X instrument (BIACORE, Uppsala, Sweden).
The data were analyzed with ProteON Manager™ 3.1 software (Bio-Rad, Hercules, CA, USA), and binding constants were determined using a 1 1 Langmuir binding model.
The data were analyzed with the ProteON Manager TM 2.1 software; binding constants were determined using the software's Langmuir model.
The five exhibiting the best apparent affinity for MMP-14 in this assay were resynthesized, purified and accurate binding constants were determined by FP analysis.
Equilibrium binding constants were determined by titrating mant-labelled nucleotides with increasing concentrations of protein and plotting the change in fluorescence (Fig. 5E and F).
The binding constants were determined from the changes in the Q-band maximum of the porphyrazine spectra at various poly (G-C) and DNA concentrations.
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