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13 - Structure and Function of Resilin
- Edited by Peter R. Shewry, University of Bristol, Arthur S. Tatham, University of Bristol, Allen J. Bailey, University of Bristol
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- Book:
- Elastomeric Proteins
- Published online:
- 13 August 2009
- Print publication:
- 30 October 2003, pp 259-278
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- Chapter
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Summary
INTRODUCTION
Biological structures with long-range elasticity are found in most animals, where they serve a number of functions, such as storing kinetic energy, absorbing shocks and vibrations, and acting as antagonists for muscles. Different groups of animals have developed different materials specialised for these purposes; insects and other arthropods have used a rubber-like, exoskeletal protein, resilin, in many places where long-range elasticity is needed.
The protein was discovered by Weis-Fogh during a study of the flight system in locusts, when he realised that energy-saving mechanisms had to be present to allow storage of kinetic energy at the end of wing strokes. A detailed analysis revealed that several elastic elements participate in such energy storage: (a) the thoracic flight muscles themselves possess a passive elastic element, which in the locust accounts for about one-third of the total elasticity of the thorax; (b) the solid, sclerotized cuticle of the thorax, which can store significant amounts of energy, although it cannot be subjected to deformations larger than 2%; and (c) some small, cuticular patches, which possess long-range elasticity, allowing them to suffer considerable deformations and to return rapidly to their equilibrium shape when the deforming forces are released; they account for about one-fourth of the total elasticity of the thorax (Weis-Fogh, 1959, 1961a). Like most other cuticular regions, these patches contain both protein and chitin, and the elastic properties reside in the protein and not in the chitin fraction.