Abstract
On the rehydration of hen egg white lysozyme activity returns at a hydration level of 0.22 h(g water/g protein) below that of monolayer coverage (0.32 h(g/g)). We explore this function of water in the resurrection of lysozyme activity by using infrared spectroscopy on sequential hydration of a previously dried enzyme. Carboxyl groups are shown to hydrate preferentially over carbonyl groups. However, the extent of hydration is dependant upon the carboxyl group either being ‘free’ or ‘ion-paired.’ These two hydration states of carboxyl groups are of importance in the mechanism of lysozyme. Associated with this process are small changes in protein structure and flexibility as monitored by Raman spectroscopy, NMR and inelastic neutron scattering. Moreover these small changes that occur just below the resurrection of activity are necessary for this event to proceed. We discuss the relevance of protein hydration in the folding and engineering of enzymes.
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