Postdoctoral Position in the Venditti Laboratory at Iowa State University

A postdoctoral position is available in the group of Vincenzo Venditti within the Department of Chemistry at Iowa State University (
The group employs a multidisciplinary approach that combines structural biology, enzymology, molecular biology, computer simulations, and protein engineering to investigate the role played by conformational disorder in regulation of large, multidomain enzymes. The systems of interest are Enzyme I (EI) of the bacterial phosphotransferase system (PTS), and the human RNA demethylases FTO and Alkbh5.

Expertise in modern biomolecular NMR and/or X-ray crystallography, as well as protein expression and purification is highly desirable.

Facilities include access to 600, 700, and 800 MHz spectrometers equipped with cryoprobes, an X-band EPR pulsed spectrometer, standard biophysical techniques (e.g. CD, ITC, SPR, fluorimeter), robots for crystallization condition screening, and all relevant equipment required for protein expression and purification.

Interested individuals are encouraged to email Dr. Venditti ( with a current CV, a list of three references, and a one-page research proposal.

Examples of the type of work on-going within the lab are given by some representative recent publications listed below.
1. Purslow, J.A., Nguyen, T.T., Egner, T.K., Dotas, R.R., Khatiwada, B., & Venditti, V. (2018). Active site breathing of human Alkbh5 revealed by solution NMR and accelerated Molecular Dynamics. Biophys. J. 115, 1895-1905
2. Nguyen, T.T., Ghirlando, R., & Venditti, V. (2018). The oligomerization state of bacterial enzyme I (EI) determines EI’s allosteric stimulation or competitive inhibition by alpha-ketoglutarate. J. Biol. Chem. 293, 2631-2639.
3. Egner, T.K., Naik, P., Nelson, N.C., Slowing, I.I., & Venditti, V. (2017). Mechanistic insights into nanoparticle surface adsorption by solution NMR spectroscopy in an aqueous gel. Angew. Chem. Int. Ed. 56, 9802-9806.
4. Venditti, V., Schwieters, C.D., Grishaev, A. & Clore, G.M. (2015). Dynamic equilibrium between closed and partially-closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering. Proc. Natl. Acad. Sci. USA 112, 11565-11570.
5. Venditti, V., Tugarinov, V., Schwieters, C.D., Grishaev, A. & Clore, G.M. (2015). Large interdomain rearrangement triggered by suppression of micro- to millisecond dynamics in bacterial Enzyme I. Nat. Commun. 6, 5960.
6. Venditti, V., Ghirlando, R. & Clore, G.M. (2013). Structural basis for enzyme I inhibition by alpha-ketoglutarate. ACS Chem. Biol. 8, 1232-1240.