European journal of solid state and inorganic chemistry vol:34 issue:7-8 pages:745-758
Pressure and temperature effects an proteins in solution can be divided into elastic and conformational components. Elastic effects can be interpreted in terms of changes in cavities and hydration. Conformational effects are the consequence of extensive changes in the secondary and tertiary structure. The spectroscopic techniques which permit to follow these effects are shortly reviewed and infrared spectroscopy is treated in more detail. Both thermodynamic and kinetic aspects of the unfolding are considered. The basis of possible biotechnological applications is discussed.