BIO

I'm a second-year student at FSU and I am originally from Des Plaines, Illinois, a suburb of Chicago. My current research interests are very broad and I am interested in studying areas across biology, chemistry, and medicine.

Determining the Structure of the N-Terminus of the Sulfite Reductase Flavoprotein

Abstract

Sulfite Reductase (SiR) is a unique protein which is responsible for turning sulfur into biomass. SiR has two types of subunits: a flavoproteins (SiRFP) and a hemoprotein (SiRFP). The N-terminus of SiRFP allows the eight SiRFP subunits to combine and form an octamer. To better understand the structure of the SiRFP octamer and SiR in general, the N-terminus’s structure must first be determined. This is difficult because the whole octamer is a large protein complex. To simplify the process, we have fused just the N-terminus of SiRFP to a smaller protein called SUMO (NFPSh). To get the N-Terminus we must first grow a culture of cells which carry the gene that express NFPSh, lyse the cells, and send the protein through various columns to purify it. Once we have the protein, we use a robotic machine called the Gryphon to test our protein under many different chemical conditions to identify the conditions in which NFPSh is inclined to crystallize. From there, we can set up manual trays with similar conditions to attempt to get the protein to form large crystals. Once the protein has been successfully crystallized, a technique called X-ray crystallography will be used to get a diffraction pattern. We can use the diffraction pattern to find the electron density and determine the structure of the protein. Once the structure has been determined, it will give insight into how the N-terminus functions to octomerize SiRFP, which will help us better understand the structure and function of the molecule, SiR.

Keywords: Crystallization, Protein Structure, X-Ray Crystallography