Resilin

Resilin is an elastomeric protein found in many insects. It is part of what enables insects of many species to jump or pivot their wings efficiently. It was first discovered by Torkel Weis-Fogh in locust wing-hinges.

Resilin is currently the most efficient elastic protein known (Elvin et al., 2005). The elastic efficiency of the resilin isolated from locust tendon has been reported to be 97% (only 3% of stored energy is lost as heat). It does not have any regular structure but its randomly coiled chains are crosslinked by di- and tri-tyrosine links at the right spacing to confer the elasticity needed to propel some jumping insects distances up to 150 times their length (as found in fleas). Resilin must last for the lifetime of adult insects and must therefore operate for hundreds of millions of extensions and contractions; its elastic efficiency ensures performance during the insect's lifetime. Resilin exhibits unusual elastomeric behaviour only when swollen in polar solvents such as water.

A recombinant form of the resilin protein of the fly Drosophila melanogaster, pro-resilin, was synthesized in 2005 by expressing a part of the fly gene in the bacterium Escherichia coli. It is expected to have many applications in the athletic footwear, medical,^[1] microelectronics and other industries.

References and external links

• "Resilin project clocks near perfect 98%". CSIRO. 
• Elvin CM, Carr AG, Huson MG, et al. (October 2005). "Synthesis and properties of crosslinked recombinant pro-resilin". Nature 437 (7061): 999–1002. Bibcode:2005Natur.437..999E. doi:10.1038/nature04085. PMID 16222249. [Insects tapped for better rubber Lay summary] – Nature News (12 October 2005). 
• Summary from University of South Australia
• Torkel Weis-Fogh: Scientific Papers and Correspondence