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 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.
PhD in Chemistry, Iowa State University, IA, USA
BS in Chemistry, Peking University, Beijing, China
Selected list of publications:
“Effects of chelator lipids, paramagnetic metal ions and trehalose on liposomes by solid-state NMR”, D. Lam, J. Zhuang, L. Cohen, B. Arshava, F. Naider, M. Tang. Solid State Nucl. Magn. Reson. 94, 1-6 (2018).
“Paramagnetic Effects on NMR Spectra of Isotropic Bicelles with Headgroup Modified Chelator Lipids and Metal Ions”,. M. Tang, K. Mao, S. Li, J. Zhuang, K. Diallo. Phys. Chem. Chem. Phys. 18, 15524-15527 (2016).
“Experimental Protein Structure Verification by Scoring with a Single, Unassigned NMR Spectrum”, J. M. Courtney, Q. Ye, A. E. Nesbitt, M. Tang, M. D. Tuttle, E. D. Watt, K. M. Nuzzio, L. J. Sperling, G. Comellas, J. R. Peterson, J. H. Morrissey, C. M. Rienstra. Structure 23, 1958-1966 (2015).
"Advanced Solid-State NMR Approaches for Structure Determination of Membrane Proteins and Amyloid Fibrils", Tang M, Comellas G, Rienstra CM. Acc. Chem. Res., 2013, 46, 2080-2088,
"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
"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.
"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.
"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.
"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.