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个人简介

(2012-2013) NIH BTRC Ultrafast Optical Processes Laboratory Staff Scientist Postdoctoral (2006-2011), University of Pennsylvania (Robin M. Hochstrasser) Ph.D. (2006), University of Pennsylvania (Feng Gai) B.S., B.A. (2000), University of Scranton

研究领域

A major thrust of my research focuses on the development and application of novel, ultrafast laser spectroscopy techniques to observe the interplay of structure and dynamics in biologically relevant systems. Femtosecond (10-15 s) laser pulses will be employed to explore new linear and nonlinear infrared spectroscopic properties of molecular systems. Initiation methods, such as optical triggering, in conjunction with two-dimensional infrared (2D IR) spectroscopy will be used to acquire atomic level structural information to generate snapshots of the structural evolution in various biophysical events. Such research provides an atomistic window into drug action, protein motion and folding events, the dynamical behavior of membrane proteins, or the fast folding of RNAs, all pivotal to combat prevalent diseases and to guide drug discovery.

近期论文

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I.M. Pazos, A. Ghosh, M. J. Tucker, F. Gai, Ester Carbonyl Vibration as a Sensitive Probe of Protein Local Electric Field, Angewandte Chemie, 2014, 53, 6080-6084. A. Ghosh, M. J. Tucker, F. Gai, 2D IR Spectroscopy of Histidine: Probing Side-Chain Structure and Dynamics via Backbone Amide Vibrations, J. Phys. Chem. B, 2014, ASAP online. DOI: 10.1021/jp411901m . J. R. Courter, M. Abdo, S. P. Brown, M. J. Tucker, R. M. Hochstrasser, A. B. Smith III, The Design and Synthesis of Alanine-Rich alpha-Helical Peptides Constrained by an S,S-Tetrazine Photochemical Trigger: A Fragment Union Approach, J. of Organic Chemistry, 2014, 79, 759-768. Tucker, M.J., Abdo, M., Courter, J.R., Chen, J., Brown, S.P., Smith III, A.B., Hochstrasser, R.M.; “Nonequilibrium Dynamics of Helix Reorganization Observed by Transient 2D IR Spectroscopy”, Proc. Natl. Acad. Sci. U.S.A. 2013, 110, 17314-17319. M. J. Tucker, M. Abdo, J. R. Courter, J. Chen, A. B. Smith III, R. M. Hochstrasser. Dicysteine S,S-tetrazine: A potential ultra-fast photochemical trigger to explore the early events of peptide/protein folding. J Photochem. Photobiol. A: Chemistry, 2012, 234, 156-163. A. Ghosh, M. J. Tucker, R. M. Hochstrasser. The identification of arginine residues in peptides by 2D-IR echo spectroscopy. J Phys. Chem. A, 2011, 115, 9731-9738. M. J. Tucker, X. S. Gai, E. F. Fenlon, S. Brewer, and R. M. Hochstrasser. 2DIR Photon Echo of Azido- Probes for Nucleic Acids. Physical Chemistry Chemical Physics, 2011, 13, 2237-2241. M. J. Tucker, J. R. Courter, J. Chen, O. Atasoylu, A. B. Smith III and R. M. Hochstrasser. Tetrazine Phototriggers: Probes of Protein Dynamics. Angewandte Chemie, 2010, 49, 3612-3616. Communication Cover Article (Highlighted in April 26, 2010 issue of Chemical and Engineering News) M. J. Tucker, A.L. Serrano, F. Gai. Direct Assessment of the alpha-Helix Nucleation Time. J Phys. Chem. B, 2011, 115, 7472-7478. M. J. Tucker, Y. S. Kim, and R. M. Hochstrasser. 2D IR photon echo study of anharmonic coupling in the OCN region of phenyl cyanate. Chemical Physics Letters, 2009, 470, 80-84. A. Ghosh, A. Remorino, M. J. Tucker, R. M. Hochstrasser. 2D IR photon echo spectroscopy reveals hydrogen bond dynamics in aromatic nitriles. Chemical Physics Letters,2009, 469, 325-330. M. M. Waegele, M. J. Tucker, and F. Gai. 5-Cyanotryptophan as infrared probe of local hydration status in proteins. Chemical Physics Letters, 2009, 478, 249-253. M. J. Tucker, R. Oyola, and F.Gai. Exploring the feasibility of using p-cyano-phenylalanine as a sensitive fluorescent probe in binding and folding. Biopolymers, 2006, 83, 571-576. M. J. Tucker, J. Tang, and F. Gai. A new method to probe the membrane-assisted helix folding dynamics. J. Phys. Chem B, 2006, 110, 8105-8109. M. J. Tucker, R. Oyola, and F. Gai. Conformational distribution of a 14-residue peptide in solution: A FRET study. J. Phys. Chem. B, 2005, 109, 4788–4785. M. J. Tucker, Z. Getahun, V. Nanda, W.F. DeGrado, and F. Gai. A new method for determining the conformation and orientation of membrane-binding peptides. J. Am. Chem. Soc., 2004, 126, 5078–5079.

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