Cellular life takes place in a dynamic, heterogeneous, constantly restructuring environment. My research group studies how the chemical reactivity of enzymes is fine tuned and regulated to operate successfully in this fluctuating environment. One central research focus in our group is the contribution of the membrane properties to the high specificity and rate enhancement of membrane enzymes. A second central theme is the biological role of selenium in proteins that utilize the rare amino acid selenocysteine. Selenoproteins signal the level of cellular oxidative stress and play a central role in regulating redox pathways. We seek to understand the key differences that set selenoproteins apart from their cysteine-containing homologues.
To experimentally address these
diverse questions my lab employs biochemical methods, solid
and solution-state nuclear magnetic resonance (NMR)
spectroscopy as well as a variety of optical microscopy
techniques ranging from single molecule total internal
reflection fluorescence (TIRF) microscopy to spectral imaging.