Figure 3
From: The non-octarepeat copper binding site of the prion protein is a key regulator of prion conversion
Comparison between copper K-edge XAS experimental data of pathological Q212P, P102L and WT HuPrP.
k3-weighted EXAFS spectra and Fourier transforms of Cu(II) and Cu(I) bound to WT HuPrP(90–231) and Q212P at pH 5.5 and 7.0 (a) and of Cu(II) and Cu(I) bound to WT HuPrP(90–231) and P102L at pH 5.5 and 7.0 (b). Schematic representations of copper binding sites in the WT HuPrP(90–231) (c) and in the mutants (d) at both pH 5.5 and 7.0. Green spheres identify a single cupper ion at both oxidative states.
