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On the structure of resilin

1965; Elsevier BV; Volume: 13; Issue: 3 Linguagem: Inglês

10.1016/s0022-2836(65)80144-9

1089-8638

G.F. Elliott, A. F. Huxley, Torkel Weis‐Fogh,

Dyeing and Modifying Textile Fibers

Structures from insects composed of the rubber-like protein resilin have been examined by high- and low-angle X-ray diffraction and in thin sections in the electron microscope. By X-ray diffraction, tendons of pure resilin, air-dried without tension, gave a diffuse unoriented ring at about 4 Å. Tendons dried under tension, at 2·6 to 3·3 times unstrained length, gave the same ring and in addition a single equatorial reflection at 4·5 ± 0·05 Å. This reflection disappeared when the tendon was returned to its unstrained length. No low-angle reflections were observed at any time. Structures composed of resilin were not penetrated by methacrylate, but sections were obtained containing patches of pure resilin surrounded by methacrylate. In the electron microscope, these sections showed that resilin treated with osmium tetroxide has a low electron-scattering power and no detectable fine structure. Small structures formed of resilin would therefore be extremely difficult to detect. Both methods show resilin to be highly amorphous, as was to be expected from its physical properties.