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. 2010 Nov 10;39(7):2483–2491. doi: 10.1093/nar/gkq984

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© The Author(s) 2010. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — Gibbs free energies of binding SS HMG boxes to their optimal and sub-optimal DNA sequences, separated into their electrostatic and non-electrostatic components using Equation (1). The protein-induced bend angles are given below the bars. Although the electrostatic component dominates the affinity in all cases, the more tightly a given HMG box binds (the more negative the total Gibbs energy), the greater is the non-electrostatic component and the larger the bend angle. As regards the relationship to the bend angle, see also (32). The DNA sequences DNA^Lef, DNA^Sry and DNA^Sox are those previously considered optimal for binding the three HMG boxes, though SRY protein binds better to DNA^Sox. Data taken from (12).