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 language | English (US) |
---|---|
Title of host publication | Proceedings of the 2010 IEEE 36th Annual Northeast Bioengineering Conference, NEBEC 2010 |
DOIs | |
State | Published - Jun 8 2010 |
Externally published | Yes |
Event | 36th Annual Northeast Bioengineering Conference, NEBEC 2010 - New York, NY, United States Duration: Mar 26 2010 → Mar 28 2010 |
Other
Other | 36th Annual Northeast Bioengineering Conference, NEBEC 2010 |
---|---|
Country/Territory | United States |
City | New York, NY |
Period | 3/26/10 → 3/28/10 |
All Science Journal Classification (ASJC) codes
- Bioengineering