You are here

Structure of reflectin protein probed by solid-state nuclear magnetic resonance

Download pdf | Full Screen View

Date Issued:
2019
Abstract/Description:
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.
Title: Structure of reflectin protein probed by solid-state nuclear magnetic resonance.
10 views
7 downloads
Name(s): Boykin, Tommy, Author
Chen, Bo, Committee Chair
Schulte, Alfons, Committee Member
Tatulian, Suren, Committee Member
Teter, Kenneth, Committee Member
University of Central Florida, Degree Grantor
Type of Resource: text
Date Issued: 2019
Publisher: University of Central Florida
Language(s): English
Abstract/Description: 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.
Identifier: CFE0007433 (IID), ucf:52712 (fedora)
Note(s): 2019-05-01
Ph.D.
Sciences, Physics
Doctoral
This record was generated from author submitted information.
Subject(s): cephalopods -- bioelectronics -- solid-state NMR
Persistent Link to This Record: http://purl.flvc.org/ucf/fd/CFE0007433
Restrictions on Access: campus 2024-05-15
Host Institution: UCF

In Collections