College: Eberly College of Science
Address: 104 Chemistry Building
Spin-labeling proteins using unnatural amino acids
We seek to develop novel structural methods aiming to resolve structures of hard-to-study misfolded and intrinsically disordered proteins. We use advanced electron paramagnetic resonance (EPR) spectroscopy to measure distances between two strategically placed spin-labels on proteins. This method provides unique information on structure and dynamics of proteins, especially in systems that are not readily accessible by conventional structural methods. Our laboratory has obtained first proof of concept for such a methodology using traditional spin-labeling methods. In the current project we aim to maximize the information that could be obtained from a single spin-labeling experiment using a variety of advanced pulse EPR methods. We predominantly explore unnatural-amino-acid-based spin probes in this research. The information gathered in this study will be used to establish protocols to resolve long-standing questions about misfolding processes associated with prion and prion-like neurodegenerative diseases such as mad-cow disease, the scrappie disease in sheep, Creutzfeldt-Jakob Disease in humans.