Dynamic light-scattering (DLS) studies are reported for lysozyme in aqueous magnesium chloride solutions
at ionic strengths 0.6, 0.8, and 1.0 M for a temperature range 10−30 °C at pH 4.0. The diffusion coefficient
of lysozyme was calculated as a function of protein concentration, salt concentration, temperature, and scattering
angle. A Zimm-plot analysis provided the infinitely-dilute diffusion coefficient and the protein-concentration
dependence of the diffusion coefficient. The hydrodynamic radius of a lysozyme monomer was obtained
from the Stokes−Einstein equation; it is 18.6 ± 1.0 Å. The difference (1.4 Å) between the hydrodynamic
and the crystal-structure radius is attributed to binding of Mg2+ ions to the protein surface and subsequent
water structuring. The effect of protein concentration on the diffusion coefficient indicates that attractive
interactions increase as the temperature falls at fixed salt concentration. However, when plotted against ionic
strength, attractive interactions exhibit a maximum at ionic strength 0.84 M, probably because Mg2+−protein
binding and water structuring become increasingly important as the concentration of magnesium ion rises.
The present work suggests that inclusion of ion binding and water structuring at the protein surface in a
pair-potential model is needed to achieve accurate predictions of protein-solution phase behavior.