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Ming Tang
Assistant Professor
College of Staten Island - City University of New York
Ph.D. Programs in Chemistry and Biochemistry, The Graduate Center of the City University of New York
Department of Chemistry
2800 Victory Blvd
Staten Island, NY 10314
Office: 6S-231
Phone: 718-982-3916
E-mail: Ming.Tang_at_csi.cuny.edu
Research Interests
- Novel Method of Membrane Protein Structure Determination
- Voltage Sensing Domains of Ion Channels
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:
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. The method will create topographic maps to provide a clear picture of the proteins in the membrane and how they change upon membrane interactions or ligand binding.
Voltage Sensing Domains of Ion Channels
To elucidate the mechanism of voltage sensing domains (VSD) of ion channels regulated by ligands and membrane composition with detailed structural information. The VSD is comprised of four transmembrane helices, known as S1, S2, S3 and S4. The S4 helix specifically has positively charged residues, usually arginines in a repeating arrangement such that there is one arginine at every third position, with hydrophobic residues in between. The conformational change responsible for channel activation is initially due to the motion of S4 outwardly away from the inside of the cell due to electrostatic interactions. This conformational switch leads to the opening of the pore region of the channel to be able to conduct sodium ions. The structural determination of the Nav VSD could provide insights as to the mechanisms in which this particular channel controls and allows the passage of sodium ions into neurons