Biochemistry

Chun Tang

Assistant Professor of Biochemistry

E-mail:tangch@missouri.edu

Office: 141 Schweitzer Hall

Mail: Biochemistry
117 Schweitzer Hall
University of Missouri
Columbia, MO 65211

Phone: 573-882-5641

Fax: 573-882-5635

Lab: 573-884-9356

Lab site: http://dynamics.missouri.edu

Educational background

Curriculum vitae

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Research summary

The Tang laboratory utilizes state-of-the-art nuclear magnetic resonance, or NMR, and various biochemical/biophysical/computational techniques to characterize macromolecular structure and dynamics in solution.

Research description

The conformations of biological macromolecules are constantly fluctuating on the µs-ms timescale, and the dynamics are coupled with processes such as enzyme catalysis, macromolecular association, protein folding and allosteric regulation. Established structural biology techniques including 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. With an increasing appreciation of the vital coupling between conformational dynamics of a macromolecule and its function, a new paradigm of structure determination is emerging in recent years that aims at obtaining a structure ensemble sampled by the subject protein.

In the quest to understand the underpinning mechanisms of biological macromolecules, the Tang laboratory applies novel NMR methods including paramagnetic relaxation enhancement (PRE), pseudo-contact shift (PCS), residual dipolar coupling (RDC) and relaxation dispersion, to characterize ensemble conformations of macromolecules in solution. In parallel, development of novel paramagnetic NMR methods is also actively pursued. Combined with low-resolution, localized approaches such as small angle scattering and fluorescence energy transfer, the macromolecular dynamics is being directly visualized in the Tang laboratory.

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. 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.

Kim, Y. C., Tang, C., Clore, G. M. and Hummer, G. (2008) Replica exchange simulations of transient encounter complexes in protein-protein association.  Proc. Natl. Acad. Sci. U.S.A. 105:12855-12860

Tang, C., Louis, J. M., Anita A., Suh, J. Y. and Clore, G. M. (2008) Visualizing transient events in N-terminal auto-processing of HIV-1 protease. Nature 455:693-696

Tang, C., Ghirlando, R. and Clore, G. M. (2008) Visualization of transient ultra-weak protein self-association in solution using paramagnetic relaxation enhancement. J. Am. Chem. Soc. 130:4048-4056.

More publications.

Employment opportunities

Postdoctoral opportunities

Research areas: Spatial and temporal characterization of macromolecular dynamics involved in protein complexes and signaling pathways.

How to apply:

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

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