An unusual protein found in squids, termed reflectin, possesses the unique ability for optical reflectivity and proton conductivity. Reflectin has the potential to become optically and electronically tunable, however, the molecular structure of reflectin has yet to be determined. Previous literature has considered using reflectin proteins as diffraction gratings, protonic transistors, and substrates for neural stem cell growth. Applying recombinant protein techniques, we purified the reflectin 4Ax4 protein. We determined the leucine, tryptophan, and threonine amino acids are in an ordered state by solid-state nuclear magnetic resonance (NMR). Knowing these ordered amino acids is possibly the key to understanding reflectin's natural optical and electrical properties. Understanding the link between reflectin's structure and electrical properties is essential to make the next generation of bioelectronic materials based on inexpensive, natural resources.
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Doctor of Philosophy (Ph.D.)
College of Sciences
Length of Campus-only Access
Doctoral Dissertation (Campus-only Access)
Boykin, Tommy, "Structure of Reflectin Protein Probed by Solid-state Nuclear Magnetic Resonance" (2019). Electronic Theses and Dissertations, 2004-2019. 6431.