Title :
Structure and elasticity mechanism of full length resilin proteins
Author :
Hu, Xiao ; Qin, Guokui ; Cebe, Peggy ; Kaplan, David L.
Author_Institution :
Dept. of Biomed. Eng., Tufts Univ. Medford, Medford, MA, USA
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.
Keywords :
Fourier transform spectra; X-ray diffraction; X-ray scattering; atomic force microscopy; biomechanics; biothermics; differential scanning calorimetry; elasticity; heat treatment; infrared spectra; molecular biophysics; molecular configurations; proteins; AFM; X-ray scattering; conformation; elasticity; full length resilin; insect; proteins; real-time Fourier transform infrared spectroscopy; resilin peptides; simple energy input method; super elastic biomaterials; synchrotron real-time X-ray diffraction; temperature-modulated differential scanning calorimetry; thermal treatment; Amino acids; Calorimetry; Elasticity; Insects; Protein engineering; Real time systems; Silicon; Surface morphology; Synchrotrons; Temperature;
Conference_Titel :
Bioengineering Conference, Proceedings of the 2010 IEEE 36th Annual Northeast
Conference_Location :
New York, NY
Print_ISBN :
978-1-4244-6879-9
DOI :
10.1109/NEBC.2010.5458182
