The CTPR8Y 16 -C 60 and CTPR8Y 16 -C 60 A hybrids also retained the -helical structure of the protein (Fig. ). More significantly, fullerene-bound protein became more resistant to thermal denaturation. With incrementally increased temperature, the free protein CTPR8Y reached midpoint denaturation at T m = 70.5 °C. The pristine C 60 -based conjugate CTPR8Y 16 -C 60 was marginally more stable, with T m = 73.0 °C, while the midpoint denaturation temperature of CTPR8Y 16 -C 60 A could not be directly determined, as the protein was not completely unfolded even at 95 °C (Fig. ). Thermal denaturation of the complex was then monitored in the presence of increasing concentrations of urea, and T m for CTPR8Y 16 -C 60 A was extrapolated to 90.0 °C (Fig. ). The observed enhancement of protein thermal stability can likely be explained by protein core stabilisation through C 60 binding.