Mortalin was produced in its folded state.

<p><b>A</b>) The CD spectrum shows that mortalin was obtained with a secondary structure composed of both α-helices and β-sheets. The secondary structure content, which was estimated by the CDNN deconvolution, is depicted into the figure (error < 5%). <b>B</b>) The intrinsic fluorescence emission (excitation λ at 295 nm) spectrum of mortalin had a λ_max value of 337 ± 1 nm and a <λ> value of 346.1 ± 0.2 nm, indicating that the single Trp residue was at least partially buried. In the presence of 8 mol.L^-1 urea, the spectrum was quenched and suffered a red shift (λ_max of 349 ± 1 nm and <λ> of 351.8 ± 0.2 nm), suggesting unfolding. <i>Inset</i>: normalized spectra. <b>C</b>) Mortalin CD spectra in the presence of the indicated ligands. <b>D</b>) Intrinsic fluorescence emission (excitation λ at 295 nm) spectra of mortalin in the presence of the indicated ligands, which led to a suppression of the fluorescence emission intensity and to a slightly blue shift in the spectra, as shown in the normalized fluorescence spectra (<i>inset</i>). These results suggested that mortalin was expressed in both its folded and functional state. Moreover, the presence of adenosine nucleotides and Mg²⁺ ions led to slight conformational changes in the mortalin structure.