Colloidal dispersions of α-crystallin proteins. - I. Small angle X-ray analysis of the dispersion structure
Résumé
The structure of colloidal dispersions of eye lens α-crystallin proteins was investigated using small angle X-ray scattering. The renormalized mean spherical approximation (RMSA), combined with a Verwey-Overbeek (VO) potential, was used to analyse the results obtained at two different ionic strengths, for concentrations up to 0.20 g/cm3. This model correctly accounts for the experimental data over a large scattering domain. It provides as best fit parameters an evaluation of the excluded volume and of the charge of the macromolecules which compares well with the values found in the literature. The adequacy of the model for the description of the interactions between α-crystallin particles is discussed. The whole of the results obtained indicate that α-crystallins, and possibly proteins in general, provide a natural source of model systems to study colloidal dispersions.
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