The most efficient elastomeric protein known, resilin is produced by a number of the large insectoid species on this planet. It was first identified and classified by the Old Earth zoologist Torkel Weis-Fogh during his studies of locusts. Having no regular cellular structure, it exhibits in indigenous species in coiled chain linked by di- and tri-tyrosine bonds, which contribute to high elasticity. Incredibly durable, resilin will operate across billions of extensions and contractions, and can be spun into strands (as some native species can). The long protein chains of resilin can be manipulated in various ways to increase resistance to heat – less than 3% of energy stored in natural resilin is lost to heat – and corrosives. Recombinant forms of resilin exhibit even more elasticity when immersed in aprotic solvents such as acetone or methylene chloride. Resilin can be harvested with little specialized equipment, either from nesting sites or the insectoids directly; demand has increased exponentially in recent years as new industrial uses for resilin are discovered. Perhaps the most important at this moment are the applications of resilin in microelectronics and robotics.