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Mechanism of resilin elasticity

Author

Listed:
  • Guokui Qin

    (Tufts University)

  • Xiao Hu

    (Tufts University)

  • Peggy Cebe

    (Tufts University)

  • David L. Kaplan

    (Tufts University)

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.

Suggested Citation

  • Guokui Qin & Xiao Hu & Peggy Cebe & David L. Kaplan, 2012. "Mechanism of resilin elasticity," Nature Communications, Nature, vol. 3(1), pages 1-9, January.
    • Handle: RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms2004
    DOI: 10.1038/ncomms2004
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    Cited by:

    1. Elio J. Challita & Prateek Sehgal & Rodrigo Krugner & M. Saad Bhamla, 2023. "Droplet superpropulsion in an energetically constrained insect," Nature Communications, Nature, vol. 14(1), pages 1-9, December.
    2. Qi Guo & Guijin Zou & Xuliang Qian & Shujun Chen & Huajian Gao & Jing Yu, 2022. "Hydrogen-bonds mediate liquid-liquid phase separation of mussel derived adhesive peptides," Nature Communications, Nature, vol. 13(1), pages 1-10, December.

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