Our lab works on elucidating structure and function of spin centers in their diverse roles in both natural and human-designed molecular systems, using Electron Paramagnetic Resonance (EPR) spectroscopy as a central tool.

Conformational landscapes of proteins and protein complexes

We are using DEER (double electron-electron resonance), an advanced EPR spectroscopy technique, to develop coarse-grain structural models of conformational landscapes in proteins and protein complexes. DEER measures absolute distances of up to 8 nm with a precision of 0.1 nm between spin labels attached to cysteine residues in site-directed mutants. With DEER, conformational equilibria and other conformational heterogeneity can be resolved and quantified. With DEER data, we can track down the structural mechanism of allosteric regulation in proteins.

Metallo- and radical enzymes

Many of the most difficult and complex chemical transformations in nature make use of redox or radical chemistry. Enzymes use transition metal ions, metal ion clusters, and very reactive organic radicals in their catalytic centers to perform difficult substrate transformations. Many of these reactions are essential to life, and some of them are pathologically relevant. We study the structural and dynamic details of these reactions to understand how these reactive paramagnetic intermediates are generated, harnessed and controlled.

EPR spectroscopy

Our research lab uses EPR spectroscopy in all its basic and advanced variants as our core technology. We are developing improved theory, software, and hardware to gain faster, more detailed and more robust data through increased sensitivity and resolution of measurements and increased reliability and ease of data interpretation.