Transparency of the lens of the eye is the result of a short range order in the packing of crystallin molecules within the fiber cells. Short range order depends on crystallin-crystallin as well as water-crystallin interactions. Light scattering measurements can provide information on the hydration of crystallins. Light scattering intensities were obtained as a function of scattering angle, concentration, and temperature on dilute solutions of , , and fractions of bovine lens crystallins. The temperature dependence of the second virial coefficient was negative for the crystallin fractions and positive for the fraction as well as that for crystallin (Wang, X., and Bettelheim, F. A.(1989) Proteins Struct. Funct. Genet. 5, 166-169). The partial molar enthalpy values of the solutions were negative for the crystallin fractions, indicating a tendency for homo- and heterodimer and -oligomer association. The enthalpy values were positive for the and fractions. The negative values of the enthalpy of solutions differentiate the crystallins from the other crystallins. The partial molar entropy values of solutions of and fractions were identical, those of the oligomeric fraction were higher, whereas those of crystallin were a magnitude larger than those of the the smaller crystallin molecules.

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