Ming Tang

Assistant Professor

Office: 6S-231
Phone: 718-982-3916
E-mail: Ming.Tang@csi.cuny.edu
Curriculum Vitae

Academic Background

Postdoctoral Research Associate, University of Illinois at Urbana-Champaign
Ph.D. Chemistry, Iowa State University
B.S. Chemistry, Peking University, Beijing, China

Research Interests

Our long-term research endeavor is to investigate the function-modulating interactions between proteins and membrane components by solving structures of membrane-associated protein complexes and aggregates. The elucidation of such structure-function relationships will contribute tremendously to our understanding of how proteins interact with lipids and/or cofactors to operate. In turn, these fundamental discoveries will translate into novel biomaterials and rationally designed therapeutic agents, since roughly 60% of all current drug targets are membrane proteins, yet structures of membrane proteins remain scant relative to their soluble counterparts. Further, understanding the interactions between amyloidogenic protein aggregates and the membrane will provide new insights into the mechanisms of neurodegenerative diseases, diabetes and bacterial infections. We are employing a variety of structural tools, such as solid-state NMR spectroscopy, solution NMR spectroscopy, X-ray crystallography and electron microscopy. In particular, we have successfully developed solid-state NMR methods to tackle the challenges of membrane proteins and protein aggregates. Hence, we will be able to obtain detailed atomistic models from the structural information to describe the fundamental principles of how the membrane influence protein functions and vice versa. These structures will lay the groundwork for the future translational research towards developing new therapeutic agents and novel biomaterials through collaborations within the institution and beyond. We are achieving these goals through the specific topics outline below:

  • Phosphoinositide Regulation of Ion Channels
    To elucidate the mechanism of how phosphoinositides (PIP2) regulate ion channels with atomically detailed structural information. PIP2 plays an important role in regulating many membrane ion channels and transporters. Inbalance of PIP2 concentrations is a basis for numerous human diseases, such as cancer, diabetes, heart disease and hypertension.

  • Amyloidogenic Protein-Membrane Interactions
    To determine the oligomeric structures of amyloidogenic proteins in the membrane. The toxcity of amyloidogenic protein aggregates is associated with numerous neurodegenerative diseases and type II diabetes.

  • Novel Method of Membrane Protein Structure Determination
    To develop new restraints for structural calculations of membrane-associated proteins using chelator lipids with paramagnetic metal ions. The changes of chemical shifts or intensities induced by paramagnetic metal ions can be translated into long-range distance restraints which are crucial for determining the tertiary structure of membrane proteins.

Selected Publications

"Advanced Solid-State NMR Approaches for Structure Determination of Membrane Proteins and Amyloid Fibrils", Tang M, Comellas G, Rienstra CM. Acc. Chem. Res., 2013, in press, (Published online, May 10, 2013).

"Structure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid Bilayer", Tang M, Nesbitt AE, Sperling LJ, Berthold DA, Schwieters CD, Gennis RB, Rienstra CM. J. Mol. Biol., 2013, 425, 1670-1682 (Published online, Feb 14, 2013)

"High-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental data" Tang M, Sperling LJ, Berthold DA, Schwieters CD, Nesbitt AE, Nieuwkoop AJ, Gennis RB, Rienstra CM. J. Biol. NMR 2011, 51, 227-233. (Published online, Sep 22 , 2011)

"Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement" Tang M, Berthold DA, Rienstra CM. J. Phys. Chem. Lett. 2011, 2, 1836-1841. (Published online, Jul 21 , 2011)

"Solid-State NMR Study of the Charge-Transfer Complex between Ubiquinone-8 and Disulfide Bond Generating Membrane Protein DsbB" Tang M, Sperling LJ, Berthold DA, Nesbitt AE, Gennis RB, Rienstra CM. J. Am. Chem. Soc. 2011, 133, 4359-4366. (Published online, Mar 4 , 2011)

"Structure and Mechanism of Beta-Hairpin Antimicrobial Peptides in Lipid Bilayers from Solid-State NMR Spectroscopy" Tang, M.; Hong, M. Mol. BioSyst. 2009, 5, 317-322. (Published online, January 29, 2009)

"Effects of Arginine Density on the Membrane-Bound Structure of a Cationic Antimicrobial Peptide from Solid-State NMR", Tang, M.; Waring, A. J.; Hong, M. Biochim. Biophys. Acta. 2009, 1788, 514-521. (Published online, November 14, 2008)

"Effects of Guanidinium-Phosphate Hydrogen Bonding on the Membrane-Bound Structure and Activity of an Arginine-Rich Membrane Peptide from Solid-State NMR", Tang, M.; Waring, A. J.; Lehrer, R. I.; Hong, M. Angew. Chem. Int. Ed. 2009, 47, 3202-3205. (Published online, March 13, 2008)

"Arg Dynamics in a Membrane-Bound Cationic Beta-Hairpin Peptide from Solid-State NMR", Tang, M.; Waring, A .J; Hong,M. Chembiochem 2008, 9, 1487-1492. (Published online, April 29, 2008)

"Phosphate-Mediated Arginine Insertion into Lipid Membranes and Pore Formation by a Cationic Membrane Peptide from Solid-State NMR" Tang, M.; Waring, A. J.; Hong, M. J. Am. Chem. Soc. 2007, 129, 11438-11446. (Published online, August 18, 2007).