Fig. 8
The comparison between the cases where the free ligand concentration is barely affected by interaction and exhausted as a result of buffering. The kinetics of multisite protein species alterations in response to step change in ligand concentration from U T0/K = 0.01 to U T1/K = 200 for two different ratios of the protein concentration to the affinities of the binding sites L T /K = 2 a for the intermediate species N 1/L T , N 2/L T and N 3/L T , b for the apo- and fully bound species N 0/L T and N 4/L T respectively) and L T /K = 50 c for the intermediate species N 1/L T , N 2/L T and N 3/L T , d for the apo- and fully bound species N 0/L T and N 4/L T respectively). The model predicts that due to the lack of available ligand and buffering by the multisite protein in the case of limited amount of ligand, the multisite protein is unable to become fully saturated after the step change in ligand, and the majority of the ligand becomes distributed among the intermediate species. e. The comparison of the dynamics of free ligand concentration U/K after step change in ligand. The amount of available ligand is barely altered for L T /K = 2, and exhausted when the ratio of total protein concentration to the binding constant is L T /K = 50