Computational analysis reveals temperature-induced stabilization of FAST-PETase

analyses additionally highlighted that the flexibility of these regions decreased at 50°C in FAST-PETase, instead of exhibiting increased flexibility at higher temperature as would be expected from thermodynamic considerations. This effect was confirmed by physical energy calculations, which suggest that temperature-dependent conformational changes of FAST-PETase decrease the free energy of unfolding (ΔG(stability)) and rigidify the enzyme at elevated temperatures enhancing stability. Looking forward, these findings might help guide the rational engineering of protein thermostability and contribute to our understanding of the thermal adaptation of thermophilic enzymes.