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  • Title: Structural basis of eye lens transparency: light scattering by concentrated solutions of bovine alpha-crystallin proteins.
    Author: Xia JZ, Wang Q, Tatarkova S, Aerts T, Clauwaert J.
    Journal: Biophys J; 1996 Nov; 71(5):2815-22. PubMed ID: 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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