Fig. 3

Structural properties of chaperone-hairpin complex. a Molecular surface representations of the binding partners colored by electrostatic potential (red, negative; blue, positive). Arrows indicate the approximate location of labeling sites. b Donor-donor (light green), acceptor-acceptor (magenta), and donor-acceptor (gray) fluorescence correlation functions for FRET-labeled NCD S2C-T65C in isolation (top), bound to the hairpin (middle), and bound to the folding-incompetent hairpin (bottom). Solid black lines are global fits of the three respective correlation functions, which are used to determine the reconfiguration times, τ_r, of the chaperone. c Mean transfer efficiencies for all labeling pairs from the mapping experiment (triangles) at 30 mM PB pH 7.0 and the coarse-grained molecular simulations (circles). Mean values are provided in the Source Data file. Labeling positions in the chaperone and the hairpin are shown in cyan and red, respectively. The uncertainties associated with transfer efficiency values are ~0.01 based on multiple simulations and ~0.03 for the experiments (error dominated by instrument calibration). d Molecular representations of the disordered nucleic acid-chaperone complex from the simulations (see Supplementary Movies 1 and 2); color code as in Fig. 1a. e Correlation between experimental and simulated mean transfer efficiencies. The dashed gray line is the identity line, the solid black line is a linear regression