The thioamide is a compelling isostere of the peptide backbone amide bond, where single atom substitution provides differing chemical and physical properties that can be used by medicinal chemists and biophysicists to probe or control protein stability. The number of known natural thioamides has grown rapidly in recent years, further motivating the study of this unusual post-translational modification. To improve the understanding of the impact of thioamide incorporation on peptide and protein structure, I have worked to characterize thioamides incorporated into β-sheet systems of varying complexities.

Performed research in Professor Casey Londergan's biophysical lab. Undergraduate thesis titled: Using the Thiocyanate Probe to Elucidate the Lipid-Bound Dynamics of N-terminally Acetylated Alpha-Synuclein.