Fig. 5: FRET efficiencies and kinetics parameters of TAD-NCBD binding.

a Bimolecular association rate constant k_a = k_B/[NCBD] (blue) and dissociation rate constant k_U (red) obtained from the extracted relaxation rate, k = k_B + k_U, and the bound fraction, p_B = k_B/k. k_B is the apparent binding rate constant. b Dissociation constant, K_d (= k_U/k_a). c–e Measured FRET efficiencies of the bound and unbound states. c E₁^2c (blue square, bound; red square, unbound) and E_1B^3c (blue circle) calculated using E_2B^2c. d E₂^2c (blue square, bound; red square, unbound) and E_2B^3c (blue circle) calculated using E_1B^2c. e E₁₂^3c (blue, bound; red, unbound) calculated using two-color FRET efficiencies E₁^2c (circle) and E₂^2c (square). Error bars are standard deviations calculated from the curvature at the maximum of the likelihood function. Source data are provided as a Source Data file.