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

► We show results on the dynamics of the folding/unfolding process of hydrated lysozyme. ► We follow the thermal and temporal behavior of hydrophilic interactions. ► The dynamic details of the process can be helpful to avoid folding alteration. ► Lysozyme should be driven along the pathway related to the correct folded structure. ► The Native state of the protein can be brought back only under precise conditions.