Abstract
Abstract 1. 1. The conformation in solution of eye-lens proteins obtained from cortical extracts of adult bovine lenses, was studied by means of the optical rotatory dispersion method. 2. 2. The rotatory data were analysed according to the modified two-term Drude equation, the Moffitt-Yang equation and the one-term Drude equation. 3. 3. The lens proteins appeared to consist of a mixture of α-helix, random coil and some other structure, which disappeared upon denaturation by acid, alkali or 8 M urea, and also in 2-chloroethanol. 4. 4. From a comparison with other proteins it seems probable that this other structure has a β conformation.
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