Fig. 5.

CD analysis of ZmFer1 protein nanocage after heat treatments. (A) CD spectra of ZmFer1 protein nanocage after heat treatment at different temperatures (60-100 °C) for 10 min, with untreated protein as a control; (B) correlation between the percentage of α-helix secondary structure calculated based on CD spectra at 208 and 222 nm; θ, observed ellipticity (mdeg); (C) The calculated average fraction of folded α-helix structures in ZmFer1 ferritin based on θ _{208 nm} and θ _{222 nm} at different temperatures (60-100 °C). Data were fitted with a Boltzmann sigmoidal model using GraphPad Prism (GraphPad Software Inc, California, USA)