title: On the dynamics of water molecules at the protein solute interfaces.
abstract: Proteins, with the large variety of chemical groups they present at their molecular surface, are a class of molecules which can be very informative on most of the possible solute-solvent interactions. Hen egg white lysozyme has been used as a probe to investigate the complex solvent dynamics occurring at the protein surface, by analysing the results obtained from Nuclear Magnetic Resonance, X-ray diffractometry and Molecular Dynamics simulations. A consistent overall picture for the dynamics of water molecules close to the protein is obtained, suggesting that a rapid exchange occurs, in a picosecond timescale, among all the possible hydration surface sites both in solution and the solid state, excluding the possibility that solvent molecules can form liquid-crystal-like supramolecular adducts, which have been proposed as a molecular basis of 'memory of water'.
authors.affiliation: Department of Molecular Biology, Biomolecular Structure Research Center, University of Siena, Via Fiorentina 1, 53100 Siena, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Bernini
authors.forename: O
authors.initials: O
authors.lastname: Spiga
authors.forename: A
authors.initials: A
authors.lastname: Ciutti
authors.forename: S
authors.initials: S
authors.lastname: Chiellini
authors.forename: N
authors.initials: N
authors.lastname: Menciassi
authors.forename: V
authors.initials: V
authors.lastname: Venditti
authors.forename: N
authors.initials: N
authors.lastname: Niccolai
mesh_terms: D000818:Animals; D002645:Chickens; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D004527:Egg Proteins / Q000378:metabolism*; D008956:Models, Chemical; D008958:Models, Molecular; D009113:Muramidase / Q000378:metabolism*; D011487:Protein Conformation; D012997:Solvents; D014867:Water / Q000378:metabolism*
chemical_list: D004527:Egg Proteins; D012997:Solvents; D014867:Water; C421864:hen egg lysozyme; D009113:Muramidase