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 μ 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 α-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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
