emad@ks.uiuc.edu
3143 Beckman Inst
Office: (217) 244-6914
Fax: (217) 244-6078
Mail to:
Beckman Institute
405 N Mathews Ave
Urbana, IL 61801
Emad Tajkhorshid
Assistant Professor of Biochemistry, Pharmacology, and Biophysics
Affiliation: Beckman Institute for Advanced Science and Technology
Education
B.S. 1989 Tehran University
Ph.D. 2001 University of Heidelberg
Postdoc. 2000-2003 Univ. of Illinois, U-C
Computational Studies of Membrane Channels and Transporters
Membrane proteins are of critical importance for all living cells. They are responsible for exchange of materials and information across cellular membranes, and participate in a wide range of metabolic, regulatory, and sensory mechanisms. My research focuses on structure function relationship of membrane proteins, in particular membrane channels and transporters, and understanding the mechanism of their function using simulation and computational methodologies. Recent advances in structural determination of membrane proteins have resulted in high resolution structures of several membrane proteins that we can use in simulation studies to understand how the architecture of the protein, and specific interactions and dynamics of its building blocks provide the basis of its mechanism of function.
Representative Publications
Tornroth-Horsefield, S., Wang, Y., Hedfalk, K., Johanson, U., Karlsson, M., Tajkhorshid, E., Neutze, R., and Kjellbom, P. 2006. Structural mechanism of plant aquaporin gating. Nature, 439:688–94. [Abstract]
Wang, Y., Schulten, K., and Tajkhorshid, E. 2005. What makes an aquaporin a glycerol channel - A comparative study of GlpF and AqpZ. Structure, 13:1107–18. [Abstract]
Amaro, R., Tajkhorshid, E., and Luthey-Schulten, Z. 2003. Developing an energy landscape for the novel function of a (β/α)8 barrel: ammonia conduction through HisF. Proc. Natl. Acad. Sci. USA, 100:7599–604. [Abstract]
Tajkhorshid, E., Nollert, P., Jensen, M.O., Miercke, L.J.W., O'Connell, J., Stroud, R.M., and Schulten, K. 2002. Control of the selectivity of the aquaporin water channel family by global orientational tuning. Science, 296:525–30. [Abstract]