Abstract

Accurate models of protein diffusion are important in a number of applications, including liquid−liquid phase separation and growth of protein crystals for X-ray diffraction studies. In concentrated multicomponent protein systems, significant deviations from pseudobinary behavior can be expected. Rayleigh interferometry is used to measure the four elements (Dij)v of the ternary diffusion coefficient matrix for the extensively investigated protein, hen egg-white lysozyme (component 1) in aqueous NaCl (component 2) at pH 4.5 and 25 °C. These are the first multicomponent diffusion coefficients measured for any protein system at concentrations high enough to be relevant to modeling and prediction of crystal growth or other phase transitions, and the first for a system involving lysozyme at any concentration. The four ternary diffusion coefficients for the system lysozyme chloride/NaCl/water are reported for lysozyme chloride at 0.60 mM (8.6 mg/mL) and NaCl at concentrations of 0.25, 0.50, 0.65, 0.90, and 1.30...

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