Sterpone, FabioBertonati, ClaudiaBriganti, GiuseppeMelchionna, Simone2011-12-162011-12-162011-12-16201010.1088/0953-8984/22/28/284113https://infoscience.epfl.ch/handle/20.500.14299/75378WOS:000279257300016The 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.ThermostabilityStabilityEnzymesHyperthermophilesClassificationFlexibilityTemperatureSequencesSurfacesBehaviortext::conference output::conference proceedings::conference paper