Postdoctoral Studies

The Einstein Postdoctoral Individual Development Plan

Job Title:

Postdoctoral Position in Laboratory of David Cowburn

Job Description:


There is an immediate opening for a postdoctoral researcher in the laboratory of Dr. David Cowburn at Albert Einstein College of Medicine, Bronx, NY, Department of Biochemistry.  This is for our projects  on (1) the molecular mechanism of rapid and selective transport in the nuclear pore complex, funded by NIH, and using NMR, biophysical chemistry, protein engineering,  and simulations (recent publications below); (2)  split inteins that mediate the protein ligation process with unprecedented speed and fidelity, creating enormous potential in protein biotechnology with applications ranging from basic molecular and cell biology to the preparation of protein therapeutics.  


You will have access to the outstanding facilities of the NYSBC, and the Einstein Structural NMR Core.  


Interested candidates with expertise (PhD, or about to complete) in biomolecular NMR and experience in protein biochemistry and biophysics should email a biographical sketch including the names of three referencesto: .  



164.          Stevens, A.J., Sekar, G., Gramespacher, J.A., Cowburn, D., and Muir, T.W. (2018). An Atypical Mechanism of Split Intein Molecular Recognition and Folding. J Am Chem Soc 140, 11791-11799.  

163.          Hayama, R., Sparks, S., Dutta, K., Hecht, L., Cabana, C., Karp, J., Rout, M.P., and Cowburn, D. (2018). Thermodynamic characterization of the multivalent interactions underlying selective translocation through the Nuclear Pore Complex. The Journal of biological chemistry 10.1074/jbc.AC117.001649 Editors’ pick. F1000 citation, PMC5868264

162.          Sparks, S., Temel, D., Rout, M., and Cowburn, D. (2018). Deciphering the 'fuzzy' interaction of FG nucleoporins and transport factors using SANS.   Structure 26, 477-484 e474, PMC5929991

161.         Warren C, Matsui T, Karp JM, Chen H-Y, Onikubo T, Cahill S, Cowburn D, Brenowitz M, Girvin M, Shechter D. Dynamic disorder of the Histone chaperone Nucleoplasmin regulates histone binding and release. Nature Communications. (2017) 8 PMC5738438

160.          Stevens AJ, Sekar G, Shah NH, Mostafavi AZ, Cowburn D, Muir TW. A promiscuous split intein with expanded protein engineering applications. Proceedings of the National Academy of Sciences of the United States of America. 2017;114 (32):8538-43. PMC5559002  

159.          Upla, P., Kim, S.J., Sampathkumar, P., Dutta, K., Cahill, S.M., Chemmama, I.E., Williams, R., Bonanno, J.B., Rice, W.J., Stokes, D.L., Cowburn, D., et al. (2017). Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25, 434-445 PMC5342941

158.          Karp, J.M., Sparks, S., and Cowburn, D. (2017). Effects of FGFR2 kinase activation loop dynamics on catalytic activity. PLoS Comput Biol 13, e1005360 PMC5313233

157.          Liu D, Cowburn D. Segmental isotopic labeling of proteins for nmr study using intein technology (2017) Methods in molecular biology. 2017;1495:131-45

156.          Khoo Y, Singer A, Cowburn D. Bias Correction in Saupe Tensor Estimation. arXiv preprint arXiv:160606975. 2016

155.          Khoo Y, Singer A, Cowburn D. Integrating nOe and RDC using sum-of-squares relaxation for protein structure determination. J Biomol NMR. 2017;68 (3):163-85

154.          Liu D, Yaun Y, Xu R, Cowburn D. Domain interactions of C-terminal Src Kinase determined through NMR spectroscopy with segmental isotope labeling. Protein and Cell. 2017; 8 , 67-71


Albert Einstein College of Medicine is an equal opportunity employer committed to workforce diversity.


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