Homeopathy 2004; 93(04): 199-202
DOI: 10.1016/j.homp.2004.07.002
Original Paper
Copyright ©The Faculty of Homeopathy 2004

On the dynamics of water molecules at the protein solute interfaces

A Bernini
O Spiga
A Ciutti
S Chiellini
N Menciassi
V Venditti
N Niccolai

Subject Editor:
Further Information

Publication History

Received20 February 2004
revised04 May 2004

accepted05 July 2004

Publication Date:
20 December 2017 (online)


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’.