Data di Pubblicazione:
1997
Abstract:
In this paper, we report dielectric spectroscopy and optical measurements on lysozyme in water-ethanol mixtures
as a function of alcohol concentration in the water-rich region of composition (cosolvent mole fraction X~<0.25).
Dielectric measurements show a well defined relaxation curve in the MHz region, from which we obtain the electric
dipole moment # and the effective hydrodynamic radius r of the protein. UV melting measurements with estimation
of the van't Hoff enthalpy are also reported. Molar ellipticity measurements were performed to test the or-helix
content. The results indicate that alcohol promotes a more tightly folded conformation of the protein. Our
measurements show a correlation between the effects of ethanol on the conformational properties of lysozyme and
changes in the properties of solvent, as inferred from previous adiabatic compressibility and IR data on water-ethanol
mixtures.
as a function of alcohol concentration in the water-rich region of composition (cosolvent mole fraction X~<0.25).
Dielectric measurements show a well defined relaxation curve in the MHz region, from which we obtain the electric
dipole moment # and the effective hydrodynamic radius r of the protein. UV melting measurements with estimation
of the van't Hoff enthalpy are also reported. Molar ellipticity measurements were performed to test the or-helix
content. The results indicate that alcohol promotes a more tightly folded conformation of the protein. Our
measurements show a correlation between the effects of ethanol on the conformational properties of lysozyme and
changes in the properties of solvent, as inferred from previous adiabatic compressibility and IR data on water-ethanol
mixtures.
Tipologia CRIS:
01.01 Articolo in rivista
Keywords:
Lysozyme; Water-ethanol; Dielectric Behaviour; CD
Elenco autori:
DE FRANCESCO, Alessio
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