Abstract
We describe the thermodynamic stability of a hyperthermophilic protein with respect to the equilibrium and kinetic aspects. The stabilization mechanism of a hyperthermophilic protein is found to be characterized by its slow unfolding and this appears to be a common characteristic of hyperthermophilic proteins. It was shown that the buried hydrophobic residues contribute to the kinetic robustness. Furthermore, we discuss whether some concepts about protein stability, which are observed in mesophilic proteins, are applicable to the hyperthermophilic protein.
https://ror.org/055n47h92 
