Structure and elasticity mechanism of full length resilin proteins

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

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

Full length resilin, as well as resilin peptides encoded by exons 1 and 3, were analyzed for structural features. The elasticity mechanisms of resilin related to insect function are described. To approach this goal, a simple energy input method based on thermal treatment was used to detail the transitions and structures of resilin. A systematic pathway to the mechanism was followed based on Temperature-modulated Differential Scanning Calorimetry (TMDSC), Real-time Fourier Transform Infrared Spectroscopy (FTIR), synchrotron Real-time X-ray, and AFM. The results revealed that the conformation and transition of resilin proteins played a critical role for their elastic mechanisms, which provided an effective pathway to design new super elastic biomaterials.

Original languageEnglish (US)
Title of host publicationProceedings of the 2010 IEEE 36th Annual Northeast Bioengineering Conference, NEBEC 2010
DOIs
StatePublished - Jun 8 2010
Externally publishedYes
Event36th Annual Northeast Bioengineering Conference, NEBEC 2010 - New York, NY, United States
Duration: Mar 26 2010Mar 28 2010

Other

Other36th Annual Northeast Bioengineering Conference, NEBEC 2010
Country/TerritoryUnited States
CityNew York, NY
Period3/26/103/28/10

All Science Journal Classification (ASJC) codes

  • Bioengineering

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