Research in the Royer group encompasses molecular and cellular biophysics. Our research is defined broadly along two axes.
First, we aim to define the conformational landscapes of proteins and how these modulate function. We are particularly interested in pressure effects on proteins, both in vitro and in vivo. Well over half of the Earths microbial biomass is found at elevated pressures, yet we do not understand how the sequences of the biomolecules in these extremophile organisms have evolved to function at pressures which disrupt their mesophilic counterparts. We also exploit pressure perturbation to explore the functional conformational landscapes of biomolecules. In these studies we use a combination of biophysical approaches such as fluorescence, SAXS and NMR coupled with variable pressure and temperature devices.
Our second major research axe is aimed at understanding the molecular basis for cell state transitions (e.g., commitment to division) and cellular responses to stresses such as changes in nutrient sources or pressure. Here we focus on transcriptional regulation. In these studies we use a combination of fluctuation microscopy, fluorescence lifetime imaging and super-resolution PALM/STORM imaging. Currently we are pursuing six major research projects:
Check out our newest publication Colman et al. Structural evolution of the ancient enzyme, Dissimilatory Sulfite Reductase, Proteins: Struct. Func. Bioinformatics 90, 1331-1345 (2022).