Pressure as a variable in biophysics/biochemistry allow the structure/function and dynamics/function relationships to be analysed in detail in various biomolecular assemblies. Overall volume changes of the biomolecule favour the dissociation of ionic interactions under pressure. Exposure to water of hydrophobic residues occurring, for instance, during protein unfolding disturbs the "loosely packed" structure of pure water and is thus favoured at high pressures. This proposal aims at investigating important aspects of the structure-to-function relationship of a well known and characterised enzyme, lysozyme, using pressure as thermodynamic variable. We are interested in investigating the evolution of the dynamics associated to structural changes, in both native and molten globule configuration, when hydrostatic pressure is applied in the range 1 - 7Kb at room temperature.