405 N. Mathews Ave.
Urbana, IL 61801
Additional Campus Affiliations
Emad Tajkhorshid is Hastings Endowed Chair in the Biochemistry Department, as well as holds additional appointments across multiple colleges that include Chemistry, Bioengineering, Pharmacology, Biophysics and Quantitative Biology, Computational Science and Engineering, and the Carle-Illinois College of Medicine at the University of Illinois. He is also a full time faculty member of the Beckman Institute for Advanced Science and Technology. He joined the faculty of the Departments of Biochemistry (LAS) and Pharmacology (UI COM) in 2007 and was fast tracked to associate professor with tenure in 2010 and then again to the rank of professor in 2013. His tenure dossier was selected as one of the two top UIUC tenure cases on campus. In 2015, Professor Tajkhorshid was named a University of Illinois Scholar, after being nominated by both UIUC and UIC campuses. In 2016, he was awarded the Faculty Excellence Award from the School of Molecular and Cellular Biology at UIUC. Later that year he was named Endowed Chair in Biochemistry. Emad Tajkhorshid directs the leads the NIH Center for Macromolecular Modeling and Bioinformatics and the Computational Structural Biology and Molecular Biophysics Group at the Beckman Institute. Dr. Tajkhorshid has authored over 200 research articles (H-index 64) with over 23,000 citations in such high profile journals as Nature, Science, Cell, eLife, and PNAS. He has delivered nearly 200 invited lectures at international meetings, universities, and research institutes. He has served on the Editorial Boards of multiple major journals, including Biophysical Journal, Journal of Biological Chemistry, PLoS Computational Biology, and Biochemical and Biophysical Research Communication.
The Tajkhorshid Group focuses on developing and applying advanced computational techniques to characterization of biological phenomena, particularly membranes and membrane proteins, with the aim of achieving the most detailed microscopic view of structural and dynamical bases underlying biological function. Major areas of his extensive research portfolio, which have enjoyed continuous support from multiple federal funding agencies (NIH, NSF, DOE, DOD) over many years, include mechanistic studies of membrane transport proteins, principles of energy transduction and coupling in bioenergetic proteins, and lipid modulation of protein function, e.g., in signaling proteins associated with the cellular membrane.
Awards and Honors
NIH Transformative Award, 2017-2022
Endowed Chair of Biochemistry, 2016-
MCB Faculty Excellence Award, 2016
University of Illinois Scholar, 2015-2018
UIUC top tenure packages of the year, 2010
Sun, C., Benlekbir, S., Venkatakrishnan, P., Wang, Y., Hong, S., Hosler, J., Tajkhorshid, E., Rubinstein, J. L., & Gennis, R. B. (2018). Structure of the alternative complex III in a supercomplex with cytochrome oxidase. Nature, 557(7703), 123-126. https://doi.org/10.1038/s41586-018-0061-y
Wen, P. C., Vanegas, J. M., Rempe, S. B., & Tajkhorshid, E. (2018). Probing key elements of teixobactin-lipid II interactions in membranes. Chemical Science, 9(34), 6997-7008. https://doi.org/10.1039/c8sc02616e
Jiang, T., Yu, K., Hartzell, H. C., & Tajkhorshid, E. (2017). Lipids and ions traverse the membrane by the same physical pathway in the nhTMEM16 scramblase. eLife, 6, [e28671]. https://doi.org/10.7554/eLife.28671
Chen, S., Zhao, Y., Wang, Y., Shekhar, M., Tajkhorshid, E., & Gouaux, E. (2017). Activation and Desensitization Mechanism of AMPA Receptor-TARP Complex by Cryo-EM. Cell, 170(6), 1234-1246.e14. https://doi.org/10.1016/j.cell.2017.07.045
Verhalen, B., Dastvan, R., Thangapandian, S., Peskova, Y., Koteiche, H. A., Nakamoto, R. K., Tajkhorshid, E., & McHaourab, H. S. (2017). Energy transduction and alternating access of the mammalian ABC transporter P-glycoprotein. Nature, 543(7647), 738-741. https://doi.org/10.1038/nature21414
Zeng, F., Chen, Y., Remis, J., Shekhar, M., Phillips, J. C., Tajkhorshid, E., & Jin, H. (2017). Structural basis of co-translational quality control by ArfA and RF2 bound to ribosome. Nature, 541(7638), 554-557. https://doi.org/10.1038/nature21053
Arcario, M. J., Mayne, C. G., & Tajkhorshid, E. (2017). A membrane-embedded pathway delivers general anesthetics to two interacting binding sites in the Gloeobacter violaceus ion channel. Journal of Biological Chemistry, 292(23), 9480-9492. https://doi.org/10.1074/jbc.M117.780197
Mansoor, S. E., Lü, W., Oosterheert, W., Shekhar, M., Tajkhorshid, E., & Gouaux, E. (2016). X-ray structures define human P2X 3 receptor gating cycle and antagonist action. Nature, 538(7623), 66-71. https://doi.org/10.1038/nature19367
Bharathkar, S. K., Parker, B. W., Malyutin, A. G., Haloi, N., Huey-Tubman, K. E., Tajkhorshid, E., & Stadtmueller, B. M. (2020). The structures of secretory and dimeric immunoglobulin a. eLife, 9, 1-29. [e56098]. https://doi.org/10.7554/eLife.56098
Chavan, T. S., Cheng, R. C., Jiang, T., Mathews, I. I., Stein, R. A., Koehl, A., McHaourab, H. S., Tajkhorshid, E., & Maduke, M. (2020). A CLC-EC1 mutant reveals global conformational change and suggests a unifying mechanism for the CLC CL– /H+ transport cycle. eLife, 9, [e53479]. https://doi.org/10.7554/eLife.53479
Chen, H., Maia, J. D. C., Radak, B. K., Hardy, D. J., Cai, W., Chipot, C., & Tajkhorshid, E. (2020). Boosting free-energy perturbation calculations with GPU-Accelerated NAMD. Journal of Chemical Information and Modeling, 60(11), 5301-5307. https://doi.org/10.1021/acs.jcim.0c00745
Ciudad, S., Puig, E., Botzanowski, T., Meigooni, M., Arango, A. S., Do, J., Mayzel, M., Bayoumi, M., Chaignepain, S., Maglia, G., Cianferani, S., Orekhov, V., Tajkhorshid, E., Bardiaux, B., & Carulla, N. (2020). Aβ(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage. Nature communications, 11(1), . https://doi.org/10.1038/s41467-020-16566-1
Dehghani-Ghahnaviyeh, S., Kapoor, K., & Tajkhorshid, E. (2020). Conformational changes of the nucleotide binding domains of P-glycoprotein induced by ATP hydrolysis. FEBS Letters. https://doi.org/10.1002/1873-3468.13992