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. Author manuscript; available in PMC: 2008 Oct 12.
Published in final edited form as: Biochemistry. 2008 Sep 17;47(40):10620–10629. doi: 10.1021/bi801157p

Figure 2.

Figure 2

PMP22 binds Cu(II) and Zn(II) at 20°C. (A) Fluorescence emission spectra of PMP22 in DPC micelles in the presence of various metal ions. The protein and metal ion concentrations were 1 μM and 1 mM, respectively. The buffer was 25 mM acetate, pH 5.5, 150 mM NaCl, 0.5 % DPC. (B) Titration with zinc acetate at pH 5.5 (open squares) and in HEPES buffer at pH 7.5 (closed circles). Single and double binding site models were fit to the data to determine dissociation constants (see Methods). Fitted Kd for Zn(II) binding were 1.4 mM at pH 5.5, and 20 μM and 3 mM at pH 7.5. (C) Titration with copper sulfate at pH 5.5. Fitted Kd were 37 μM and 1.1 mM.