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. 2008 Jan 21;36(5):1567–1577. doi: 10.1093/nar/gkm1176

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© 2008 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — IcaR–DNA binding determined by ITC. Representative plots from an ITC experiment are shown with raw data in the upper panel and curve fit in the lower panel. The IcaR protein was titrated into the reaction cell containing the 28E dsDNA. Note that the first addition was 3/8 the volume of the other additions. The first two data points were not used in the fitting. Thermodynamic values obtained from the curve fit are: ΔS = 84.3 cal/mol K, ΔH = 13.8 ± 0.2 kcal/mol, K_B = 2.0 ± 0.8 × 10⁸ M^–1, N = 2.18 ± 0.01. N is the stoichiometry of bound IcaR dimer per dsDNA.