Mechanism of resilin elasticity

Guokui Qin, Xiao Hu, Peggy Cebe, David L. Kaplan

Research output: Contribution to journalArticlepeer-review

101 Scopus citations

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 structureĝ€"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.

Original languageEnglish (US)
Article number1003
JournalNature communications
Volume3
DOIs
StatePublished - 2012

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

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