Fluorescence is the process by which the fluorophore absorbs a stimulus like light on interaction. This causes a conformational change in the fluorophore where a longer wavelength is created via an energy transfer process. The lower emission of photons through the change can be detected as an electrical signal. This phenomena can be seen in aromatic biological proteins like tryptophan and tyrosine through the imidazole ring, allowing them to be synthesized in an array of environments Williams, Slatko
specifically target the tumor. To help solve these challenges, Ce6 was conjugated to carbon dot (Cdot). This helps Ce6 be more water soluble and extend the half life in the blood. Additionally, Cdot indirectly excites Ce6 by Forster fluorescence resonance energy transfer. Cdot is also nno-cytotoxic, and has a cheap
myoglobin, to model the impact of ionic liquids on human tissue. I use visible light, circular dichroism, and fluorescence spectroscopy, as well as Förster resonance energy transfer (FRET) and kinetic absorbance assays developed by my lab to monitor the unfolding of myoglobin in ionic liquid environments. Using these data, I calculated the Gibb’s free energy of the functional protein in the presence of each ionic liquid, to compare their relative stabilities. In the year that I have worked on this project