Dielectric and gravimetric studies of water binding to lysozyme.
Time domain dielectric spectroscopy and hydration isotherm measurements as a function of temperature have been applied to hydrated lysozyme powder. Two dielectric dispersions were identified, the first centred at approximately 8 MHz and a second above 1 GHz. The higher dispersion is considered to be the result of rotational relaxation of water molecules bound to the enzyme. In this case the results indicate the existence of a population of 32 water molecules per lysozyme molecule which are irrotationally bound to the lysozyme structure. A larger population of water molecules is relatively free to respond to the electric field and exhibits a dipole moment close to that of vapour phase water molecules. Multi-temperature hydration isotherm measurements are used to calculate enthalpies and entropies associated with the binding of water to lysozyme. Discontinuities both in dielectric and in thermodynamic characteristics in the range 10-14% hydration are interpreted as a re-ordering of the water structure on the enzyme surface.
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Institute of Molecular and Biomolecular Electronics, University of Wales, Bangor, Gwynedd, UK.
D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D002645:Chickens; D004563:Electrochemistry; D019277:Entropy; D066298:In Vitro Techniques; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D013816:Thermodynamics; D014867:Water
D014867:Water; D009113:Muramidase