My research is centered around (1) the development of Cu(II)-based site-directed spin-labeling (SDSL) for Electron Paramagnetic Resonance (EPR)-based distance measurements and (2) applying these techniques to answer fundamental questions about protein-DNA interactions. SDSL methodologies allow for the incorporation of stable unpaired electrons at specific sites of a protein or DNA. When two or more unpaired electrons are incorporated, EPR can measure the distance between the two unpaired electrons with angstrom resolution. Additionally, these measurements are crucial for studying protein systems that are too large for NMR-based experiments or too complicated to be crystallized for X-ray crystallography.
Our group has pioneered Cu(II)-based SDSL that are rigid and small. As a result, the Cu(II) distances primarily reflect the motions of protein or DNA in solution. These distances allow for observation of conformational changes and elucidate the assembly of large oligomers. Specifically, I use distance measurements to observe protein-DNA interactions in solution to shed light on structural principles that govern highly-specific sequence-specific DNA recognition.
Education: BA, Biochemistry, University of Montana, 2017
PhD Advisor: Dr. Sunil Saxena
Department of Chemistry
723 Chevron Science Center
219 Parkman Ave
Pittsburgh, PA 15260
email: ZIH12 [at] pitt.edu