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. 2014 Jan 13;289(9):5528–5533. doi: 10.1074/jbc.M113.537068

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© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 1. — Comparison of equilibrium dissociation binding constants (K_d) obtained by stopped-flow fluorometry (NCBD_Y2108W/ACTR_WT (a) and NCBD_Y2108W/ACTR_L1049A (b)) and isothermal titration calorimetry (NCBD_Y2108W/ACTR_WT (c) and NCBD_Y2108W/ACTR_L1049A (d)). Observed rate constants (k_obs) are plotted against the concentration of ACTR, and from the fitting (12), the apparent association rate constant of binding (k_on^app) is obtained. The insets show a trace in a displacement experiment in which a preformed NCBD_Y2108W/ACTR solution was mixed with an excess of NCBD_WT to obtain the apparent dissociation rate constant (k_off^app). Stopped-flow data shown in a are from Dogan et al. (7), and data shown in b are from Dogan et al. (8). The two different methods produced the same K_d.