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 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.
Xia
J Z
JZ
Department of Biochemistry, University of Antwerp, U.I.A., Belgium.
Wang
Q
Q
Tatarkova
S
S
Aerts
T
T
Clauwaert
J
J
D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D002417:Cattle; D003459:Crystallins / Q000737:chemistry*; D004058:Diffusion; D007908:Lens, Crystalline / Q000737:chemistry*; D008027:Light; D008954:Models, Biological; D012542:Scattering, Radiation; D012996:Solutions; D014461:Ultracentrifugation
D003459:Crystallins; D012996:Solutions