Fig. 6
Kinetics of multisite protein species alterations for a protein with significantly different association constants. The kinetics of multisite protein species was investigated in response to step change of ligand from U 0/K = 0.001 to U 1/K = 8 and to U 1/K = 400 for the intermediate (N 1/L T , N 2/L T and N 3/L T in a, c) as well as apo- and fully bound conformations (N 0/L T and N 4/L T in b, d), respectively, in the case of significantly different association h 1 = 1, h 2 = 0.6, h 3 = 0.2, h 4 = 0.1 and the same dissociation constants h −1  = h −2  = h −3  = h −4  = 1. The comparison with the kinetics of the protein with slightly different association constants suggests that in this case the species acquire a degree of asynchronous dynamics