Fig. 4: Real-time monitoring of interactions between c-Myc and small molecule inhibitors. | Nature Communications

Fig. 4: Real-time monitoring of interactions between c-Myc and small molecule inhibitors.

From: Visualizing single-molecule conformational transition and binding dynamics of intrinsically disordered proteins

Fig. 4: Real-time monitoring of interactions between c-Myc and small molecule inhibitors.

a, b Real-time current trajectories (time resolution of 17 μs) in 50 μM 10074-A4 (a) and PKUMDL-YC-1205 (b) solutions (0.01× PBS, 5% DMSO, pH = 7.4). The left column is real-time current data over 60 s, the middle column is an enlarged image of the green-marked area, and the right column is an enlarged image of the blue- (a) or purple- (b) marked area. c Chemical structures of the inhibitors 10074-A4 (blue, racemic mixture in the experiments) and PKUMDL-YC-1205 (purple). d Population of Myc-inhibitor binding states at different inhibitor concentrations (n = 3, number of the devices, data are presented as mean values ± SD). The dissociation constants of the inhibitors were obtained by fitting the Hill equation (Supplementary Table 6). Source data are provided as a Source Data file.

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