James J. ChouDepartment of Biological Chemistry and Molecular Pharmacology
Harvard Medical School
Seeley G. Mudd Building, Room 109
240 Longwood Avenue, Boston, MA 02114
tel: (617) 432-2920; fax: (617) 432-2921
Our research is to extend the limit of solution NMR spectroscopy in the structural study of membrane proteins, not only by developing novel methods but also applying them to the interesting yet unsolved mysteries in the world of membrane. Systems of primary interest to us are small viral ion channels and fusion peptides, nucleic acid transport pores, and apoptosis regulatory proteins. We have recently developed a powerful method that incorporates the small bicelles, which provide a natural environment for solubilizing membrane proteins, and residual dipolar couplings (RDCs), which yields valuable orientation restraints for structure calculation. In combination with the classic NOE-based technology, the RDC approach has brought solution NMR spectroscopy to a new level as a tool for protein structure determination. Available projects in the lab are: 1) structural and dynamic characterization of the M2 viral channel of Influenza A for understanding the H+ channel gating mechanism; 2) structural study of NID67, a small membrane protein preferentially induced by the nerve growth factor; 3) probing the membrane-bound state of tBID, a proapoptotic protein connecting the TNF/Fas receptor activation to mitochondrial damage.
Chou, J.J., Li, H., Salvesen, G.S., Yuan, J., and Wagner, G. (1999). Solution Structure of BID, an Intracellular Amplifier of Apoptotic Signaling. Cell 96, 615-624.
Chou, J.J., Li, S., Klee, C.B., and Bax, A. (2001). Solution structure of Ca2+-calmodulin reveals flexible hand-like properties of its domains. Nature Struct. Biol. 8, 990-997.
Chou, J.J., Kaufman, J.D., Stahl, S.J., Wingfield, P.T., and Bax, A. (2002). Micelle-Induced Curvature in a Water-Insoluble HIV-1 Env Peptide Revealed by NMR Dipolar Coupling Measurement in Stretched Polyacrylamide Gel. J. Am. Chem. Soc. 124, 2450-2451.
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