The protein in the oothecal glands of praying mantids (Sphodromantis tenuidentata, Miomantis monacha) exists in the form of lamellar liquid crystalline spherulites, which coalesce as they flow out of a punctured gland tubule. Electron micrographs of sections of these spherulites after fixation show parabolic patterns of an electron-light component, set in a continuous matrix of protein. Such patterns arise in helicoidal systems (e.g. arthropod cuticle) and microdensitometric scans of the matrix show a rhythmical electron-density variation consistent with helicoidal structure. Double spiral patterns identical to those seen in liquid crystal spherulites are illustrated. These properties resemble those of cholesteric liquid crystals. The constructional units appear to be molecular rather than fibrillar as described by previous authors. The helicoidal architecture arises by self-assembly in the gland lumen. Lamellar surface structures self-assembled spontaneously on glass coverslips when the protein was left to stand for several days. When heated to 55 °C, the birefringent liquid crystalline protein abruptly changes to an isotropic gel, with associated loss of parabolic patterning in electron micrographs and of the rhythmical electron-density variation on microdensitometric scans. This behaviour is compared to the formation of gelatin from collagen, in terms of the randomization of an originally ordered secondary structure.
Investigation of the Electron Density Variation During the 21 August 2017 Solar Eclipse
