Postdoctoral Position, Johns Hopkins School of Medicine: NMR of enzymatic systems

The Frueh lab in the Johns Hopkins School of Medicine, Department of Biophysics and Biophysical Chemistry is offering a post-doctoral position to investigate enzymatic assembly lines with nuclear magnetic resonance (NMR) with a flexible starting date in early 2017. The candidate should have graduated in or after 2014.

We are interested in motivated, independent candidates with demonstrated expertise in biomolecular NMR who are also versed in protein production and purification. The post-doctorant will benefit from our strong expertise in both NMR (applied and theoretical) and biochemistry/biophysics. Priority will be given to candidates who either (i) master the product operator formalism and can code state-of-the-art pulse sequences or (ii) have expertise in biochemical/enzymatic assays, in particular those related to nonribosomal peptide synthetases or similar (FAS, PKS). The laboratory operates its own 600 MHz Bruker spectrometer, equipped with a QCI cryoprobe and nitrogen liquefier unit, and we are a major user of the Hopkins NMR facility: 800 MHz, two 600 MHz, two 500 MHz. In addition, the laboratory has access to extensive departmental equipment (ITC, MALS, DLS, SAXS, etc.) and facilities (MS, synthetic chemistry, etc.). The candidate should be a team player who will embrace the collegial and dynamic framework of the Johns Hopkins Medical Institute. 

Project description:

Our laboratory has a dual purpose: we design NMR methods and study the molecular mechanisms of nonribosomal peptide synthetase domain communication. NRPSs employ a conserved modular, multi-domain organization to produce pharmaceutically active metabolites (penicillin, bacitracin, etc.). This organization resembles an assembly-line where simple substrates are covalently tethered to sequential modules and condensed to form complex natural products. Our primary focus is to understand the interplay between synthetic steps and domain communication. Towards this aim, we use NMR to characterize fleeting molecular events (Goodrich et al. Biochemistry 2015, Goodrich et al. J Am Chem Soc 2015). The dynamic nature of NRPSs and their large molecular weight stimulates method developments to overcome spectroscopic challenges (Harden et al. J Am Chem Soc 2014, Harden et al. J Mag Res 2015). Within this environment, the post-doctorant will study the structures, dynamics, kinetics, and binding affinities of partner NRPS domains and test novel NMR methods.

See also ,

Interested candidates should submit a CV and a personalized cover letter, as well as either the name and contact information of two references, or two letters of references, to: .