(co-advised with Prof. M. Ashley Spies)

Sophie is fascinated by how tiny molecular machines (proteins!) change shape as they interact with DNA and small molecules in our cells; work that helps reveal how drugs can better target these dynamic systems. She uses single-molecule biophysics to watch individual proteins in action, uncovering mechanisms relevant to genome maintenance and drug design. When she’s not in the lab, you can find her traveling, doing yoga, on an adventure with her husky (Haichi!), or debating which horror movie reigns supreme (self-proclaimed connoisseur of all things spooky).

Projects:

Sophie studies how dynamic proteins help maintain genomic stability and how their movements can be harnessed for drug discovery. Using her single-molecule toolkit — including smTIRF, smFRET, CTFM, and mass photometry — she explores how the DNA-binding protein Replication Protein A (RPA) and its variant forms manage fragile, repetitive DNA sequences linked to neurodegenerative diseases. In a complementary project, she investigates glutamate racemase (MurI), an essential bacterial enzyme, to understand how small molecules alter its native dynamics and inhibit its function, guiding the design of new antibiotics.