page_title: Resilin
section_title: Secondary structure
hierarchical_section_title: Resilin / Composition of resilin / Secondary structure
caption_attribution_description: English: The mechanism of action of resilin before and after loading
context_page_description: Resilin is an elastomeric protein found in many insects and other arthropods. It provides soft rubber-elasticity to mechanically active organs and tissue; for example, it enables insects of many species to jump or pivot their wings efficiently. Resilin was first discovered by Torkel Weis-Fogh in locust wing-hinges.
  Resilin is currently the most efficient elastic protein known. The elastic efficiency of the resilin isolated from locust tendon has been reported to be 97%. 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 38 times their length. 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 behavior only when swollen in polar solvents such as water.
  In 2005, a recombinant form of the resilin protein of the fly Drosophila melanogaster was synthesized by expressing a part of the fly gene in the bacterium Escherichia coli.
context_section_description: Resilin is a disordered protein; however its segments may take on secondary structures under different conditions. It is discovered that peptide sequence encoded by exon 1 exhibit an unstructured form and cannot be crystallized, which allows the peptide sequence segment to be very soft and highly flexible. Exon 3 encoded peptide takes on the unstructured form before loading, but transforms to an ordered beta-turn structure once stress is applied. Meanwhile, segment encoded by exon 2 serves as a chitin binding domain. It is proposed that as stress is applied, or there is energy input, exon 1 encoded peptide responds immediately due to its high flexibility. Once this occurs, the energy is passed onto exon 3 encoded peptide, which transforms from the unstructured form to beta-turn structure to store energy. Once the stress or energy is removed, exon 3 encoded segment reverses the structural transformation and outputs the energy to exon 1 encoded segment.
  Another secondary structure exon 1 and exon 3 corresponding peptides may take on is the polyproline helix (PPII), indicated by the high occurrence of proline and glycine in these 2 segments. The PPII structure widely exists in elastomeric proteins, such as abductin, elastin, and titin. It is believed to contribute in the self-assembling process and the elasticity of the protein. The elastic mechanism of resilin is proposed to be entropy related. Under relaxed state, the peptide is folded, and possesses a large entropy, but once it is stretched out, the entropy decreases as the peptide unfold. The coexistence of PPII and beta-turn play an important role of increasing entropy as resilin returns to its disordered form. The other function of PPII is to facilitate self-assembling process: it is found that the quasi-extended PPII is able to interact through an intermolecular reaction, and initiate the formation of fibrillar supramolecular structure.
caption: The Mechanism of Action of resilin
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