Solid state NMR investigation of protein-based biomaterials. Resilin : an extremely efficient elastomeric protein

• Main Author: Reddin, Andrew L. C.
• Language: English
• Published: University of British Columbia 2012
• Online Access: http://hdl.handle.net/2429/42215

Solid state nuclear magnetic resonance experiments were performed in order to investigate the microscopic properties of three resilin/resilin-like proteins: An16, rec1-resilin, and natural resilin in dragonfly tendons. Three different types of experiments were performed: measurements of chemical shifts in carbon-13 spectra, measurements of residual quadrupole couplings in deuterated water absorbed in the samples, and measurements of proton residual dipole couplings based on the buildup of multiple quantum coherences. The results suggest that the molecular chains in the materials tested are primarily randomly coiled and lacking in regular structure, and are able to easily change between many transient conformations. These conformations can vary significantly in terms of their structural characteristics, resulting in a broad distribution of localized dynamics. When stretched, An16 showed a slightly increased tendency to adopt beta-sheet secondary structure. The natural resilin also exhibited slightly more rigid structure than the other materials, which may be related to greater efficiency in the natural crosslinking process.