A Nuclear Magnetic Resonance study of the reversible denaturation of hydrated lysozyme

The understanding of the physical processes that occur below the threshold of protein thermal denaturation is of fundamental importance. In this thermal region proteins undergo a reversible folding/unfolding process whose evolution depends upon temperature and time. When the kinetics of the folding is altered, the specific biological activity of the protein is altered as well and aggregation phenomena usually intervene. The most important role in driving these processes is played by the solvent and water is certainly the solvent par excellence. It is well known that proteins become biologically active with no less than a water monolayer covering their surface. The knowledge of the physical properties of this monolayer is of basic importance to prevent folding alterations. We present a proton Nuclear Magnetic Resonance study at very high resolution of the thermodynamic properties of lysozyme hydration water as a function of temperature and time in the thermal region of the reversible denaturation.