Fig. 2: Single-molecule FAD titration. | Nature Communications

Fig. 2: Single-molecule FAD titration.

From: The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments

Fig. 2

a Histograms of population of dCRY states vs. degree of folding in the presence of varying FAD concentrations. Unfolded, intermediate and folded states are shaded in light red, light blue and gray. b Fraction of dCRY states (U unfolded, I intermediates, and F folded) plotted as a function of FAD concentration. The folded fraction, F, which is assumed to be bound to FAD, was fitted to a single site binding isotherm to obtain an apparent dissociation constant, Kd,app = 0.11 ± 0.01 nM (Section Analysis of Single-Molecule Trajectories in Methods). (N = 6 biologically independent samples per FAD concentration (i.e., 6 different single molecules evaluated), for a total of 3039 data points. Data are presented as mean values ± SD (standard deviation). Source data are available as a Source Data file.

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