Summary
In this paper we present a small-angle neutron scattering measurement on concentrated aqueous solutions of lysozyme. The ranges for the pH and for the ionic strength of the solutions are chosen in order to match the physiological values at which the enzymatic activity of the protein is at his maximum. The net charge has been determined by separate tritation experiment. The form factor and the structure factor were extracted from the experimental data. The structure factor is quantitatively reproduced within a hard-sphere model with an attractive Yukawa-tail potential. The importance in this kind of systems of the attractive interaction, even at far from zero net charge is highlighted.
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Wanderlingh, U., Giordano, R. & Giunta, G. Structure in protein solution changing the pH. Nouv Cim D 16, 1493–1498 (1994). https://doi.org/10.1007/BF02462034
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DOI: https://doi.org/10.1007/BF02462034