STRUCTURAL BASIS OF EYE LENS TRANSPARENCY - LIGHT-SCATTERING BY CONCENTRATED-SOLUTIONS OF BOVINE ALPHA-CRYSTALLIN PROTEINS

Short range order of the crystallins does account for the transparency of the eye lens, To explain the solution structure of this highly con centrated protein solution on a quantitative basis, the hydrodynamic s tructure and the interparticle interactions of the proteins have to be known. For that purpose, the light scattering of concentrated solutio ns of alpha-crystallin has been studied. Starting from the detailed kn owledge of the solution parameters of alpha-crystallin in diluted solu tions, the structure of concentrated solutions up to 360 mg/ml has bee n studied using light scattering. Our results indicate that subtle cha nges in the macromolecular structure such as optical anisotropy or str uctural asymmetry for part of the alpha-crystallins, which results in solute light-scattering heterogeneity, can dramatically increase the l ight scattering by the alpha-crystallins and cause solution opacity.