Department of Chemistry
The molecular details that define the structure, stability and function of interesting proteins and protein complexes, and those that dictate how proteins fold and interact with one another, are the focus of the research in the Urbauer laboratory. We employ an approach combining modern biophysical and molecular biology techniques. Advanced biomolecular NMR spectroscopy is emphasized, and is used to analyze the structures of proteins at high resolution and to study their dynamics and stabilities. For example, we have used NMR to solve the structure of a dimeric regulator of prokaryotic transcription regulation, and are currently using site-directed mutagenesis along with analytical ultracentrifugation, fluorescence spectroscopy, and other biophysical measurements to characterize comprehensively the contributions of individual amino acids to the stability and reactivity of the protein. Our core projects include the study of gene regulation and novel regulators of transcription initiation in bacteria, calcium signaling mediated by the quintessential and ubiquitous calcium signaling protein calmodulin, and nuclear hormone receptor activation. These projects are important fundamentally, and they are relevant for biomedical concerns including antibiotic target development, oxidative stress and biological aging, and diseases such as breast cancer.