抄録
The structure, stability, and function of dihydrofolate reductase from a deep-sea bacterium, Moritella profunda, are compared with those from Escherichia coli to briefly demonstrate the thermodynamic principles of hydrostatic pressure, which affects the structural stability and function of proteins in solution. The results clearly indicate the importance of hydration on the molecular adaptation of proteins to extreme environments such as high or low temperatures, acidic or alkaline solutions, high salinity, and high hydrostatic pressure.
