Analysis of secondary and tertiary structures of AaHMGB1 proteins.

<p>(A) CD spectra of AaHMGB1 (black line), ΔC (red line), ΔQC (green line) and ΔAQC (blue line) were performed at 25°C. Spectra were averaged from three scans at a 30 nm/min speed recorded from 190 to 260 nm, and the buffer baselines were subtracted from their respective sample spectra. (B) AaHMGB1 (black line), ΔC (red line), ΔQC (green line) and ΔAQC (blue line) were analyzed using fluorescence spectroscopy, either in the absence (native state, solid lines) or presence of 8 M urea (denatured state, dashed lines), in order to evaluate tertiary structure content. The excitation wavelength was fixed at 280 nm and the emission spectrum was recorded from 300 nm to 420 nm. Experiments were performed at 25°C.