Abstract
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.
Notes
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Graduation Date
2019
Semester
Spring
Advisor
Chen, Bo
Degree
Doctor of Philosophy (Ph.D.)
College
College of Sciences
Department
Physics
Degree Program
Physics
Format
application/pdf
Identifier
CFE0007433
URL
http://purl.fcla.edu/fcla/etd/CFE0007433
Language
English
Release Date
5-15-2024
Length of Campus-only Access
5 years
Access Status
Doctoral Dissertation (Open Access)
STARS Citation
Boykin, Tommy, "Structure of Reflectin Protein Probed by Solid-state Nuclear Magnetic Resonance" (2019). Electronic Theses and Dissertations. 6431.
https://stars.library.ucf.edu/etd/6431