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. Author manuscript; available in PMC: 2013 Jul 24.
Published in final edited form as: J Am Chem Soc. 2013 Feb 25;135(9):3613–3619. doi: 10.1021/ja312314b

Figure 4.

Figure 4

Influence of the oxygen-to-sulfur substitution in the DNA phosphate group interacting with Lys57. (a) 15N longitudinal relaxation of Lys side-chain NH3+ groups at the protein-DNA interfaces of Complexes I and II. Lys57 NH3+ group exhibited substantially different relaxation upon the oxygen-to-sulfur substitution in the DNA phosphate group. 15N relaxation of the other NH3+ groups (interacting with normal phosphate group in both complexes) was virtually unaffected. (b) Binding isotherm as monitored with fluorescence arising from a rhodamine attached to the 5’-terminus of DNA. Fractions of bound DNA calculated from the fluorescence anisotropy data at varying concentrations of HoxD9 homeodomain are plotted for Duplexes I and II.