My research focused on creating a protein that can bind to ribose and give a fluorescent signal, allowing you to quantify the amount of ribose in a sample or cell. Ribose is important to study because it is used in the creation of nucleotides in the cell, but not much is known about the amount of ribose in cells or how it is metabolized. The mechanic by which the protein can sense ribose is Forster resonance energy transfer, or FRET. Two chromophores are inserted into ribose binding protein, each of which can absorb light of a certain wavelength and emit light at a different wavelength. The chromophores are selected so that the emission wavelength of one is the same as the absorbance wavelength of the other. When they are close enough together, exciting the first chromophore causes a chain reaction that leads to light being emitted by both chromophores. However, when they are far enough apart, less light is transferred from the first to second. Since ribose binding protein changes shape when it binds to ribose, the chromophores can be placed such that it gives off a FRET signal when ribose is bound but a much weaker signal when it is not. Working ribose sensors have been created using cyan and yellow chromophores, but I attempted to develop one that used green and red.