Short range order of the crystallins does account for the transparency of the eye lens. To explain the solution structure of this highly concentrated protein solution on a quantitative basis, the hydrodynamic structure and the interparticle interactions of the proteins have to be known. For that purpose, the light scattering of concentrated solutions of α-crystallin has been studied. Starting from the detailed knowledge of the solution parameters of α-crystallin in diluted solutions, the structure of concentrated solutions up to 360 mg/ml has been studied using light scattering. Our results indicate that subtle changes in the macromolecular structure such as optical anisotropy or structural asymmetry for part of the α-crystallins, which results in solute light-scattering heterogeneity, can dramatically increase the light scattering by the α-crystallins and cause solution opacity.
Xia, J. Z., Wang, Q., Tatarkova, S., Aerts, T., & Clauwaert, J. (1996). Structural basis of eye lens transparency: Light scattering by concentrated solutions of bovine α-crystallin proteins. Biophysical Journal, 71(5), 2815–2822. https://doi.org/10.1016/S0006-3495(96)79477-8