Abstract
Studies of pressure-adapted (piezophilic) protein have lagged behind the investigation of other extremophilic proteins, however the recent characterization of proteins from deep-sea organisms has substantially accelerated the field. Recent experiments on proteins from deep-sea sources have contributed to our understanding of protein adaptation to high pressure. These studies have also complemented previous work that had investigated the effect of pressure on the activity and stability of “normal”, unadapted proteins. Together this research has lead to the conclusion that volume changes due to the hydration effects of exposed side chains and large internal cavities drive protein unfolding under high pressure.
