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. Author manuscript; available in PMC: 2011 Nov 30.
Published in final edited form as: Biochemistry. 2011 Jul 13;50(32):6920–6932. doi: 10.1021/bi200498q

Figure 12.

Figure 12

Stoichiometry of binding of FITC-MIIA1904–1927 to wt-S100A4. (A) Fluorescence anisotropy measurements of wt-S100A4 binding to MIIA1904–1927 demonstrated that wt-S100A4 has an approximately 7-fold increased affinity for FITC-MIIA1904–1927 as compared to FITC-MIIA1909–1923. Values represent the mean ± standard deviation from two or three independent titrations. (B) Stoichiometry of binding of wt-S100A4 to FITC-MIIA1904–1927. wt-S100A4 binds to FITC-MIIA1904–1927 at a 1:1 molar ratio (wt-S100A4 dimer:peptide). Gray dotted lines represent the linear regression of the rise and plateau of the titration curve. Values represent the mean ± standard deviation from two or three independent titrations.