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Biophysical Journal 71: 2815-2822 (1996)
© 1996 the Biophysical Society

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

J Z Xia, Q Wang, S Tatarkova, T Aerts and J Clauwaert

Department of Biochemistry, University of Antwerp, U.I.A., Belgium.

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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Copyright © 1996 by the Biophysical Society.