Molecular basis of eye lens transparency. Osmotic pressure and X-ray analysis of alpha-crystallin solutions.
Short range, liquid-like order of the crystallin proteins accounts for eye lens transparency. The relationship between structural and thermodynamic properties of eye lens was further investigated using osmotic pressure and small-angle X-ray scattering measurements of calf lens alpha-crystallins. The consistency of both data sets confirms that the macroscopic thermodynamic properties are determined by the structural properties accessible to X-ray scattering. In addition, the experimental data were correctly accounted for using a model developed in liquid-state physics: the rescaled mean spherical approximation combined with a Verwey-Overbeek potential. This model provides as best fit parameters the excluded volume, the charge and the diameter of an "equivalent" particle that compare well with the corresponding values found in the literature for alpha-crystallins. As a result, transparency may now be expressed as a function of a few structural parameters, the role of which is discussed. The approach presented here may be extended to studies of the thermodynamic-structural relationships of other protein solutions.
Vérétout
F
F
Centre de Génétique Moléculaire, CNRS, Gif sur Yvette, France.
Delaye
M
M
Tardieu
A
A
D000818:Animals; D002417:Cattle; D003459:Crystallins; D007908:Lens, Crystalline; D008958:Models, Molecular; D008962:Models, Theoretical; D009997:Osmotic Pressure; D013816:Thermodynamics; D014961:X-Ray Diffraction
D003459:Crystallins