title: Water around thermophilic proteins: the role of charged and apolar atoms.
abstract: 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.
authors.affiliation: Department of Chemistry, Ecole Normale Superieure, 24 rue Lhomond, 75231 Paris Cedex 05, France.
authors.forename: Fabio
authors.initials: F
authors.lastname: Sterpone
authors.forename: Claudia
authors.initials: C
authors.lastname: Bertonati
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Briganti
authors.forename: Simone
authors.initials: S
authors.lastname: Melchionna
mesh_terms: D001665:Binding Sites; D003198:Computer Simulation; D006358:Hot Temperature; D008956:Models, Chemical; D008958:Models, Molecular; D044367:Phase Transition; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D012996:Solutions / Q000737:chemistry*; D055672:Static Electricity; D013499:Surface Properties; D014867:Water / Q000737:chemistry*
chemical_list: D011506:Proteins; D012996:Solutions; D014867:Water