In this paper, a small-angle neutron scattering study of yII-crystallins near their isoelectric point is presented. The experiments were carried out using protein concentrations of 5.7-85.7 mg/ml at temperatures in the range 11 -60°C. The experimental data were analyzed using an ellipsoidal model for intraparticle correlations and the mean spherical approximation for interparticle correlations. Our studies revealed that yII-crystallins have a thick hydration layer, which is possibly due to the special arrangement of polar and ionic groups on their surface. The temperature scan shows that, as a result of relatively strong attractive forces, clusters of two, three, or higher oligomers are present below 20°C. Our results suggest that protein clusters, with a distinctive hydration layer, form a protein-rich phase that separates from a protein-lean phase as the temperature is decreased below some threshold value.
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