Hydration of lysozyme as observed by infrared spectrometry

Abstract

Infrared spectra of a film of lysozyme 3 mum thick, immersed in an atmosphere displaying a relative humidity, or hygrometry, which spans the whole range from 0 to 1 at room temperature, are recorded. The evolution of the spectra with this relative humidity is quantitatively analyzed on the basis of a newly proposed method. It allows the precise measurement of the quantity of water that remains embedded inside the dried sample at each stage of hydration, and the definition, in terms of chemical reactions of the three hydration mechanisms that correspond to the three hydration spectra on which all experimental spectra can be decomposed. With respect to preceding similar studies, some refinements are introduced that allow improvement of the interpretation, but that also raise some new questions, which mainly concern the structure of the hydrogen-bond network around the carbonyl peptide groups.