Mechanism of resilin elasticity

Guokui Qin, Xiao Hu, Peggy Cebe and David L. Kaplan ()
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Guokui Qin: Tufts University
Xiao Hu: Tufts University
Peggy Cebe: Tufts University
David L. Kaplan: Tufts University

Nature Communications, 2012, vol. 3, issue 1, 1-9

Abstract: Abstract Resilin is critical in the flight and jumping systems of insects as a polymeric rubber-like protein with outstanding elasticity. However, insight into the underlying molecular mechanisms responsible for resilin elasticity remains undefined. Here we report the structure and function of resilin from Drosophila CG15920. A reversible beta-turn transition was identified in the peptide encoded by exon III and for full-length resilin during energy input and release, features that correlate to the rapid deformation of resilin during functions in vivo. Micellar structures and nanoporous patterns formed after beta-turn structures were present via changes in either the thermal or the mechanical inputs. A model is proposed to explain the super elasticity and energy conversion mechanisms of resilin, providing important insight into structure–function relationships for this protein. Furthermore, this model offers a view of elastomeric proteins in general where beta-turn-related structures serve as fundamental units of the structure and elasticity.

Date: 2012
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DOI: 10.1038/ncomms2004

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