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. 2015 Oct 10;43(18):8856–8867. doi: 10.1093/nar/gkv864

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© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 4. — Equilibrium analysis of DNA elongations induced by flex-Ru2 intercalation. (A) Measured equilibrium flex-Ru2/DNA length expressed as an occupancy (Θ, relative to the saturated values of Figure 2) as a function of ligand concentration (C) for the forces of 20, 30 and 50 pN (red, green and blue). Fits to Equation (12) (lines) determine the binding constant K_d for each force. (B) The ratio of the fast and slow elongation amplitudes, dx_f/dx_s, as a function of C (20 pN: red, 30 pN: green and 50 pN: blue). Fits of these data points to Equation (15) (lines) determine K_d1(F). (C) Binding constants K_d1 (cyan), K_d (magenta) and K₂ (gold) versus force, as obtained from the fits of the data in Figure 4A and B to Equation (10) (lines), with K₂ calculated as K₂ = K_d1/K_d. Fitted zero-force binding constants and the flex-Ru2/DNA length changes associated with each K are collected in Table 2.