Job openings. Specific, active posts can be found below.
Students can reach our lab via applications in the Program in Molecular Biophysics, the Chemistry-Biology Interface program, and the Biochemistry, Cellular, and Molecular Biology programs. If you are at Hopkins but in a different program you may still have access to our lab, check with your program director.
We always welcome motivated post-doctoral applicants who apply for fellowships prior to joining us. Contact the P.I. if you are certain you are a good fit for the lab, and we can discuss proposals.
Interested candidates should send a CV *and* 1-2 paragraphs describing their interest in the lab to:
Dominique Frueh (email@example.com)
Johns Hopkins University School of Medicine
Department of Biophysics and Biophysical Chemistry
725 N. Wolfe Street, WBSB 713
Baltimore, Maryland 21205
POST-DOC NMR methods/Enzymes FRUEH LAB
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 2020.
We are looking for motivated, independent candidates with demonstrated expertise in biomolecular NMR, with an understanding of product operator formalism, and preferably versed in protein production and purification. The post-doctorant will benefit from our strong expertise in both NMR (applied and theoretical) and biochemistry/biophysics.
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, we have access to extensive departmental equipment (CryoEM, X-ray, 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.
Our laboratory has a dual purpose: we design NMR methods and determine dynamic molecular mechanisms in nonribosomal peptide synthetase domain communication (Frueh, Nature 2008). NRPSs employ a dynamic multi-domain organization to produce pharmaceutically active metabolites (penicillin, bacitracin, etc.). This organization resembles an assembly-line where simple substrates are covalently tethered and condensed to form complex natural products. Our focus is to understand the interplay between synthetic steps and domain communication. We use in situ biochemistry 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. Met Mol Bio 2018, Kancherla Concepts MR 2017/2018). Within this environment, the post-doctoral fellow will study the structures, dynamics, kinetics, and binding affinities of partner NRPS domains and test novel NMR methods.
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: