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13 - Structure and Function of Resilin

Published online by Cambridge University Press:  13 August 2009

Peter R. Shewry
Affiliation:
University of Bristol
Arthur S. Tatham
Affiliation:
University of Bristol
Allen J. Bailey
Affiliation:
University of Bristol
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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.

Type
Chapter
Information
Elastomeric Proteins
Structures, Biomechanical Properties, and Biological Roles
, pp. 259 - 278
Publisher: Cambridge University Press
Print publication year: 2003

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