Structure and elasticity mechanism of full length resilin proteins

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.