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'.
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|Titolo:||On the dynamics of water molecules at the protein solute interfaces.|
|Citazione:||Bernini, A., Spiga, O., Ciutti, A., Chiellini, S., Menciassi, N., Venditti, V., et al. (2004). On the dynamics of water molecules at the protein solute interfaces. HOMEOPATHY, 93(4), 199-202.|
|Appare nelle tipologie:||1.1 Articolo in rivista|