A plot of anion concentration versus absorbance at 445 nm yielded a binding curve for each interaction.
Figure 1B shows binding curves for the interaction between each peptide and the most phosphospecific TRAP (i.e., shows the highest discrimination between the phosphorylated and nonphosphorylated peptides), as monitored by fluorescence anisotropy.
The binding curves for lipo2-J3 and lipo3-J3 were distinct from each other, indicating that their interactions with gp140 were qualitatively different with superior avidity for lipo3-J3.
Figure 5b shows 16 graphs, showing the results for one typical protein kinase per graph, with each graph having three actual binding curves for the same three different drugs: bosutinib, dasatinib, and imatinib.
Saturable binding curves for cholesterol, stearic acid, arachidonic acid, and DHA were observed and the dissociation constant Kd determined for each ligand to reveal Kd values of 7 ± 1 nM, 80 ± 9 nM, 22 ± 1 nM, and 46±± 6 nM, respectively at a single site that was not necessarily the same for each ligand.
Averaged binding curves for the interaction between Ad and varying CYP11A1 concentrations were fitted simultaneously using the 1 1 Langmuir-binding model.
Figure 5 shows representative binding curves for the CYbU, A6U and the ND7-550 interactions.
We compared the binding curves for two preparations of β2GPI and for β2GPI-DV in the absence and in the presence of the dimerizing antibodies.
As a variation to the above-described equilibrium binding experiments, binding curves for ADP or ATP to chip-immobilized yeast Hsp82 or Hsp82N were obtained in the presence of raloxifene and 4-OHT.
The theoretical y values calculated using the Hill equation
