Abstract

Laser Raman spectra of the intact capsulated living lenses from chick and pigeon are reported. Evidence is presented that the First Important Soluble Crystallin (FISC) protein exists chiefly in the α-helical conformation, in contrast with the lens proteins from bovine and dogfish (mixtures of β-pleated and unordered structures). The occurrence of this low thiol protein in the α-helical form may explain the failure of the bird lens to develop cold cataract or a firm nucleus. The circular dichroism (CD) curve of chick lens proteins also indicate the presence of α-helical form. The overall “helix-forming potential” as calculated by the method of Chou and Fasman is high, supporting our Raman spectroscopic conclusion.

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