抄録
The thermo-stabilization mechanisms of proteins from hyperthermophiles have been thermodynamically elucidated on the basis of protein structures. It focuses on the electrostatic interaction due to ionizable residues unevenly distributed in hyperthermophile proteins and on the denatured structures in equilibrium with the native structures under the physiological conditions. The understanding of the denatured structures under physiological conditions should contribute to studies on folding problems and protein stability.
