Exploring the Effect of Preferential Hydration on the Dynamics of Lysozyme in Glycerol-Water Solutions

ORAL

Abstract

The relaxation processes of the protein lysozyme in glycerol-water solutions were studied with Dielectric Spectroscopy and Dynamic Light Scattering (DLS) in a wide temperature range. Analysis of the dielectric spectra revealed three relaxation processes: protein rotation, large scale protein motions (slow $\delta $-relaxation), and solvent $\alpha $-relaxation. Analysis reveals a decoupling of protein dynamics from the solvent relaxation. These effects were also studied by comparing the protein diffusion as measured by DLS and the viscosity of solutions. Both spectroscopic techniques suggest preferential hydration of the protein in solution.

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Authors

  • Krista G. Freeman

    Cleveland State University

  • Alexander Agapov

    Polymer Science Department, University of Akron, Akron, OH 44325-3909, University of Akron

  • Kiril A. Streletzky

    Cleveland State University

  • Alexei Sokolov

    Chemical Sciences Division, ORNL and Chemistry Department, University of Tennessee, Knoxville, TN 37996-1600, Chemical Sciences Division, ORNL and Dept. of Chemistry, University of Tennessee, Knoxville, TN, University of Tennessee, Knoxville, University of Tennessee, Chemical Sciences Division at ORNL, Oak Ridge, Tennessee 37837, Chemical Sciences Division, Oak Ridge National Laboratory and Chemistry Department, University of Tennessee, Knoxville, TN 37996-1600