Protein’s exist upon a delicate energy landscape where multiple states are within several kJ of one another. While current structural techniques characterize the lowest energy conformation, the higher energy states remain obscured. However, recently NMR techniques have been developed which allows one to infer structural information about these excited states. With that in mind, my interests involve structurally investigating protein ensembles and discovering how regulation and drug binding are manipulated by conformational interexchange.
Padua RA*, Sun Y*, Marko I, Pitsawong W, Stiller JB, Otten R, Kern D Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2 Nature Communications (2018) 9, 4507
Vy Nguyen*, Christopher Wilson*, Marc Hoemberger, John B. Stiller, Roman Agafonov, Steffen Kutter, Justin English, Douglas Theobald, Dorothee Kern Evolutionary drivers of thermoadaptation in enzyme catalysis. Science (2017) 355(6322):289-294