Fig. 3: Real-time monitoring of the Myc-Max interaction.

a Real-time trajectory over 60 s of the Myc-Max interaction process and a histogram of the current data (time resolution of 17 μs). b Magnification of current signal patterns; Myc folding process from the blue marked area in (a), and the Myc*-Max binding process from the red marked area in (a). The horizontal marks show the different stages during the interaction: green for the interacting folding process; blue for encounter intermediate ensemble, Myc*; and red for the fully folded binding complex. c Histogram of current data as a function of DQ47 concentration (DQ47 is the region of Max that interacts with Myc). Red indicates Myc*, blue indicates the binding state, and yellow and green indicate partial folding states. d Population of the Myc-Max bound state at different DQ47 concentrations and different pHs (red for pH 7.4 and dark red for pH 6.5, n = 3, number of the devices, data are presented as mean values ± SD). Dissociation constants were derived from the Hill equation (Supplementary Table 4). e The rate constant k at different temperatures (Arrhenius diagram, red and blue for binding and dissociation process). The activation energy of binding and dissociation were obtained by fitting the Arrhenius equation (n = 3, number of the devices, data are presented as mean values ± SD). f Equilibrium constants of the Myc*-Max binding process at different temperatures. The enthalpy change and entropy change of the dissociation process were obtained by linear fitting (n = 3, number of the devices, data are presented as mean values ± SD). Source data are provided as a Source Data file.