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

Biophys J. 1996 Nov;71(5):2815-22. doi: 10.1016/S0006-3495(96)79477-8.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biophysical Phenomena
  • Biophysics
  • Cattle
  • Crystallins / chemistry*
  • Diffusion
  • Lens, Crystalline / chemistry*
  • Light
  • Models, Biological
  • Scattering, Radiation
  • Solutions
  • Ultracentrifugation


  • Crystallins
  • Solutions