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 language | American English |
|---|---|
| Article number | 1003 |
| Journal | Nature communications |
| Volume | 3 |
| DOIs | |
| State | Published - 2012 |
ASJC Scopus subject areas
- Chemistry(all)
- Biochemistry, Genetics and Molecular Biology(all)
- Physics and Astronomy(all)