Water around thermophilic proteins: the role of charged and apolar atoms.

The thermal response of three proteins with mesophilic, thermophilic and hyperthermophilic character hints at the essential role played in thermostability by the protein-water interface. The formation of spanning water clusters enveloping the macromolecule and their resistance to thermal stress is shown to correlate with the charge distribution at the protein surface; in particular our findings suggest an effective role of the superficial charge distribution in stabilizing the global connectivity of the hydration water.