Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4924
Title: On the dynamics of water molecules at the protein solute interfaces.
Authors: Bernini, A
Spiga, Ottavia 
Ciutti, A
Chiellini, S
Menciassi, N
Venditti, V
Niccolai, Neri 
Keywords: Protein hydration, water dynamics, water memory, water-solute interaction
Issue Date: 2004
Project: None 
Journal: HOMEOPATHY
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'.
Description: 
37187
URI: http://hdl.handle.net/20.500.12779/4924
ISSN: 1475-4916
DOI: 10.1016/j.homp.2004.07.002
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