Post-Doc Position in Structural Biophysics Postdoctoral position available for highly motivated candidate in the Levinson Laboratory in the Department of Pharmacology at the University of Minnesota, Twin Cities campus. The Levinson Lab studies allostery and drug recognition in protein kinases using advanced biophysical spectroscopy coupled with structural and biochemical methods. A core focus of the lab is understanding the allosteric basis for how drug binding to the active site modulates kinase protein-protein interactions in cancer. Our projects are performed in close collaboration with the lab of David D. Thomas in the Department of Biochemistry, Molecular Biology, and Biophysics, whose time-resolved fluorescence methodology for tracking protein conformational changes is a core component of our experimental toolkit. Successful applicants will work in a highly collaborative environment that spans the disciplines of structural biology, biophysics, and biochemistry and will be exposed to a wealth of techniques from X-ray crystallography and cryoEM to optical spectroscopy and magnetic resonance.
Available projects include: 1) real-time tracking of ligand-driven allosteric structural transitions in kinases using time-resolved FRET and NMR
2) dissection of oncogenic kinase scaffolding interactions using X-ray crystallography, cryo-EM, NMR, EPR and FRET
3) allosteric drug discovery using a novel high-throughput screening platform based on nanosecond time-resolved FRET
Example recent papers: Majumdar et al., Nat Chem Biol (2021) Lake et al., PNAS (2018) Ruff et al., eLife (2018) Cyphers et al., Nat Chem Biol (2017)
Requirements - Ph.D. in biophysics, biochemistry, or a related field -Strong communication and interpersonal skills -Aptitude for working in a collaborative team
Preferred Qualifications -Experience with recombinant protein expression, particularly in insect cells and/or mammalian cells. -Familiarity with biomolecular spectroscopy, including fluorescence, infrared spectroscopy, and magnetic resonance -Familiarity with single particle cryo-electron microscopy
Our group studies allosteric regulation mechanisms that are disrupted in cancer, with a particular focus on the protein kinases. We use biophysical approaches to tease apart how allosteric regulation works and aim to harness this knowledge in pursuit of new allosteric inhibitors.
The University of Minnesota, founded in the belief that all people are enriched by understanding, is dedicated to the advancement of learning and the search for truth; to the sharing of this knowledge through education for a diverse community; and to the application of this knowledge to benefit the people of the state, the nation, and the world.