Dielectric Behavior of Lysozyme and Ferricytochrome-c in Water/Ethylene-Glycol Solutions

A. Bonincontro, S. Cinelli, G. Onori, A. Stravato

Research output: Contribution to journalArticlepeer-review


This work deals with a dielectric study at radio frequencies of the influence at room temperature of two organic molecules, known as cryo-protectants, ethylene-glycol and glycerol, on conformational and dynamic properties of two model proteins, lysozyme (lys) from chicken egg-white and ferricytochrome-c (cyt-c) from horse heart. Cyt-c is a compact globular protein whereas lys is composed of two structural domains, separated by the active site cleft. Measurements were carried out at the fixed temperature of 20°C varying the concentration of the cosolvent up to 90% w/w. From the analysis of the dielectric relaxation of the protein solution, the effective hydrodynamic radius and the electric dipole moment of the protein were calculated as a function of the cosolvent concentration. The data show that glycerol does not modify significantly the conformation of both proteins and cyt-c is also stable in the presence of ethylene-glycol. On the contrary ethylene-glycol strongly affects the dielectric response of lysozyme denoting a specific effect on its conformation and dynamics. The data are coherently interpreted hypothesizing that glycol molecule wedges between and separates the two domains of lys making them rotationally independent.

Original languageEnglish
Pages (from-to)1118-1123
Number of pages6
JournalBiophysical Journal
Issue number2
Publication statusPublished - Feb 2004

ASJC Scopus subject areas

  • Biophysics


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