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Thermal denaturation of rF20 polypeptides assessed by circular dichroism spectroscopy. Denaturation profiles were recorded at 204 nm, and the proteins were considered as 100% denatured at 95 °C. For all proteins analyzed, 50% denaturation was observed at similar temperatures between 71 and 77.5 °C (crossing point of the horizontal and vertical lines), indicating that the mutations did not have a profound effect on the overall structural stability of the polypeptide.
