Chun Tang

Assistant Professor of Biochemistry

Email:	tangch@missouri.edu
Phone:	(573) 882-5641
Fax:	(573) 882-5635
Mailing Address:	Biochemistry 117 Schweitzer Hall University of Missouri-Columbia Columbia, MO 65211
Research Areas:	Spatial and temporal characterization of macromolecular dynamics involved in protein complexes and signaling pathways
Webpage:	http://dynamics.missouri.edu

Educational Background

BS		Zhejiang University	Hangzhou, China	Biology
PhD		University of Maryland	Baltimore, Md.	Biochemistry

Research Description

The conformations of proteins and other macromolecules are fluctuating on the µs-ms timescale, and the dynamics are usually coupled with processes such as macromolecular association, protein folding and allosteric regulation. Established structural biology techniques, NMR and X-ray crystallography, are routinely used to solve the structure of the most populated species, i.e. the ground state, of a macromolecule. Two new solution NMR techniques have been developed to elucidate the macromolecular dynamics both spatially and temporally. Paramagnetic relaxation enhancement (PRE), arising from an unpaired electron, is highly sensitive to the low-occupancy species and is uniquely suited to characterize the excited-state structure. Relaxation dispersion, through studying the contribution of chemical exchange to the relaxation rates, can identify residues that participate in the conformational fluctuation and yield information on the exchange timescale.

Using the PRE technique, we have previously detected and characterized 1) the ensemble distribution of binary protein encounter complexes that lead up to a final stereospecific complex, and 2) the structure of minor partially closed form of the apo maltose-binding protein in a rapid exchange with the ground-state open form. The research in my group will be mainly devoted to these three areas: 1) detection and characterization of assembly intermediates, seeding processes, and pathways for the spontaneous oligomerization of retroviral capsid proteins; 2) detection of long-range contacts and "structural" characterization of naturally disordered proteins using joint refinement against PRE and other biophysical observables; 3) structural and dynamics investigation of rigid-body domain motion, substrate recognition and membrane association of lipidated kinases involved in apoptotic signaling cascade. In parallel, method development of paramagnetic NMR and magnetic imaging will be pursued.

Selected Publications

Tang, C., Ndassa, Y. and Summers, M. F. (2002) Structure of N-terminal 283-residue fragment of the HIV-1 Gag protein. Nat. Struct. Biol. 9: 537-543.

Tang, C., Loeliger, E., Kinde, I., Kyere, S., Mayo, K., Barklis, E., Sun, Y., Huang, M. and Summers, M. F. (2003) Antiviral inhibition of the HIV-1 capsid protein. J. Mol. Biol. 327: 1013-1020.

Tang, C., Loeliger, E., Luncsford, P., Kinde, I., Beckett, D. and Summers, M. F. (2004) Entropic switch regulates myristate exposure in the HIV-1 matrix protein. Proc. Natl. Acad. Sci. U.S.A. 101: 517-522.

Tang, C., Williams, D.C., Ghirlando, R. and Clore, G.M. (2005) Solution structure of enzyme IIA^Chitobiose from the N,N'-diacetylchitobiose branch of the Escherichia coli phosphotransferase system. J. Biol. Chem. 280: 11770-11780.

Tang, C. and Clore, G.M. (2006) A simple and reliable approach to docking protein-protein complexes from very sparse NOE-derived intermolecular distance restraints. J. Biomol. NMR 36: 37-44.

Tang, C., Iwahara, J. and Clore, G. M. (2006) Visualization of transient encounter complexes in protein-protein association. Nature 444: 383-386.

Tang, C., Schwieters, C. and Clore, G. M. (2007) Open to closed transition in apo maltose-binding protein visualized by paramagnetic NMR. Nature 449: 1078-1082.

Employment Opportunities

Post-Doctoral and Technician Opportunities

Electronic submission is encouraged, e-mail to biochemsearch@missouri.edu

Applicants should send CV and names of two references to:
Dr. Chun Tang
Postdoctoral Application
Biochemistry
117 Schweitzer Hall
University of Missouri-Columbia
Columbia, MO 65211

Solution NMR, structural biology and biophysics