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. 1996 Nov;71(5):2815–2822. doi: 10.1016/S0006-3495(96)79477-8

Structural basis of eye lens transparency: light scattering by concentrated solutions of bovine alpha-crystallin proteins.

J Z Xia 1, Q Wang 1, S Tatarkova 1, T Aerts 1, J Clauwaert 1
PMCID: PMC1233767  PMID: 8913618

Abstract

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 alpha-crystallin has been studied. Starting from the detailed knowledge of the solution parameters of alpha-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 alpha-crystallins, which results in solute light-scattering heterogeneity, can dramatically increase the light scattering by the alpha-crystallins and cause solution opacity.

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Selected References

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