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’.
Keywords
Protein hydration - water–solute interaction - water memory - water dynamics
