Life Science (Ecology, Evolution, Molecular Biology, Biomedical)
Faculty Mentor Primary Department
Department of Physics
Year of Presentation
Project Abstract, Summary, or Creative Statement
Many aquatic organisms have developed complex optical structures giving them the advantage to modulate light to manipulate their color to blend in with their surroundings. Cephalopods, in particular, are notable for their ability to camouflage themselves. Structural proteins, known as reflectin, found in the Hawaiian bobtail squid, Euprymna scolopes, were discovered to be responsible for their exceptional capabilities in camouflaging and proton conductivity, making them a promising foundation for biologically-inspired devices. However, the underlying self-assembly mechanism at the molecular level is still unknown. In this study, the second conserved domain of reflectin, termed ref2cx4, is expressed, purified, and investigated through the use of ssNMR to determine its secondary structure. Chemical shifts observed through 2D 13C-13C spectra obtained from ssNMR residue type assignments show the secondary structure Tyr, Thr, Pro, Asn, Gly, Arg, Phe, and Ser are found in an alpha-helix conformation. In contrast, Asp and Met are found in the beta-sheet conformation. 3D-NCACX and 3D-NCOCX spectra will be obtained for better resolution signals to allow sequential assignments, needed to resolve the complete structure of the protein.
Reflectin, Secondary Structure, ssNMR, Cephalopods
Probing the Secondary Structure of Intrinsically Disordered Squid Reflectin Protein Through ssNMR