Postdoc in protein dynamics at Univ. North Carolina, U.S.A

Postdoctoral position for solution NMR studies of enzyme dynamics, allostery, and engineered allosteric proteins  -- The University of North Carolina at Chapel Hill

 

A postdoctoral position is available for NMR studies of protein dynamics and allostery in the lab of Andrew Lee at the University of North Carolina at Chapel Hill (https://pharmacy.unc.edu/andrew-lee-lab/ ). Two projects have recently been funded by the NIH. The first is to investigate intersubunit communication in human and bacterial forms of thymidylate synthase (60-70 kDa), as well as to characterize dynamic conformational changes in the human form which is targeted by drugs in several cancers. NMR spectroscopy and other biophysical methods (ITC, x-ray crystallography, MD simulations) will be used to gain mechanistic understanding of allosteric and dynamic processes. The second project is to use NMR methods to determine the basis for allosteric function in engineered allosteric switch proteins. Candidates are sought with expertise in any one or more of the areas including:  protein structural biology and biophysics, protein biochemistry/enzymology, and NMR spectroscopy. These projects will employ advanced protein NMR techniques appropriate for large proteins, including NMR spin relaxation, to be carried out in a world-class, recently constructed biomolecular NMR facility. In addition, the projects are collaborative and take advantage of the expertise at UNC. Chapel Hill (and neighboring Carrboro) is a charming university town, and the growing Research Triangle area provides a stimulating environment with a wealth of opportunities. Interested individuals should contact Professor Andrew L. Lee, in the UNC Eshelman School of Pharmacy, at drewlee@unc.edu