"Profiling cysteine reactivity in complex proteomes" Eranthie Weerapan Boston College
- 10/19/2012 | 3:00 PM – 4:00 PM
- Location: Druckenmiller Hall, Room 020
- Event Type: Seminar
- Sponsor: Chemistry
- Contact: Penny Westfall
- - Open to the Bowdoin Community -
Cysteine-mediated protein activities comprise proteases, kianses, oxidoreductases and metabolic enzymes that rely on cysteine residues for catalysis and regulation. These functional cysteine residues demonstrate heightened reactivity relative to non-functional cysteines, and are sensitive to a myriad of oxidative protein modifications that serve to regulate protein activity in vivo. We are applying chemical proteomic technologies to identify cysteines that are susceptible to posttranslational modifications such as S-nitrosylation, with the goal of discovering and functionally characterizing novel sites of protein regulation. We are also developing libraries of cysteine-reactive small molecules to selectively perturb subsets of cysteine-mediated protein activities in cells. We hope these small molecule probes and mass spectrometry techniques will allow us to identify and modulate disease-relevant proteins that rely on key cysteine residues for function.