FIGURE 2.

CD spectroscopy and titration with EDTA and ZnSO₄ of recombinant Andes virus G1 tail CCHC-region (residues 543–599), which was expressed and purified under native conditions, showed that Zn²⁺-binding is required for the proper folding of this domain. Native G1 tail zinc finger domain showed a folded CD spectrum (open squares). Titration with an excess of EDTA resulted to an unfolded peak (at 204 nm) and reduced the helical peak (at 222 nm) (closed squares). The addition of 2.5 and 5 mm ZnSO₄ yielded folded CD spectra (triangles and circles).