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EnglishProteins, 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'.
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.
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| Titolo: | On the dynamics of water molecules at the protein solute interfaces. |
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| 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. |
| Anno: | 2004 |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
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http://hdl.handle.net/11365/3774
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