Fang, Chong

Education:

• Post Doctoral Fellow, Department of Chemistry, University of California, Berkeley 2007-2010
• Ph.D., Physical Chemistry and Biophysics, University of Pennsylvania 2006
• BS, Chemistry and Computer Application, University of Science and Technology of China (USTC) 2001

Awards:

• Graduate Student Travel Award, Division of Chemical Physics, APS (2006)
• SAS Dean's Scholar, University of Pennsylvania (2005)
• Outstanding undergradguate Thesis Award, USTC (2001)
• Guo Moruo Scholarship, USTC (2000)
• Outstanding Student Scholarship, Shanghai Baosteel Education Fund (1999)
• Outstanding Interdisciplinary Student Scholarship, Japan Utilities Communication Network (1998)

Research Group Website: http://oregonstate.edu/colleges/chem/fang

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Research Interests:

The central theme of Dr. Fang's research is to investigate the structure-function relationship of biomolecules, ranging from flourescent proteins which can light up subcellular entities for bioimaging to proteins and enzymes that are potential drug targets for biomedicine.  The interplay between chemistry, physics and biology greatly facilitates the ultrafast spectroscopic advances in the molecular vibration domain, which include the newly developed FSRS (femtosecond stimulated Raman spectroscopy) annd 2D IR (two-dimensional infrared spectroscopy).  The real-time structural snapshots of functional biomolecules "in action" offer unprecedented mechanistic insights on the intrinsic timescale (10fs-1ps) critical for their specific functions.  In particular, photoswitchable flourescent proteins will be studies by FSRS to reveal the characteristics of the vicinity of the chromophore, and the choreography of the "flexible" cromophore inside the protein pocket upon photoexcitation and photoquenching.

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Representative Publications:

• Chong Fang and Richard A. Mathies (2010) “Ultrafast internal conversion of solvated GFP chromophore by femtosecond stimulated Raman”, in preparation
• Mapping GFP structure evolution during proton transfer with femtosecond Raman spectroscopy.  Nature, 2009, 462, 200-204.  [Inside Green Flourescent Protein: The vibration that powers the classic gene expression marker.  Nature, 2009, 462 (7270), Editor's Summary and Cover Image.] 
• Two-dimensional infrared spectra reveal relaxation of the nonnucleoside inhibitor TMC278 complexed with the HIV-1 reverse transcriptase.  Proc. Natl. Acad. Sci. USA, 2008, 105 (5), 1472-1477.
• From the Cover: 2D infrared and optical spectroscopy, in Multidimensional Ultrafast Spectroscopy Special Feature.  Proc. Natl. Acad. Sci. USA, 2007, 104 (36), Cover Image.
• Amide vibrations are delocalized across the hydrophobic interface of a transmembrane helix dimer.  Proc. Natl. Acad. Sci. USA, 2006, 103 (45), 16740-16745.
• Two-dimensional infrared spectra of the ¹³C=¹⁸O isotopers of alanine residues in an α-helix.  J. Phys. Chem. B, 2005, 109 (39), 18652-18663.
• Two-dimensional infrared spectroscopy of isotopomers of an alanine rich α-helix.  J. Phys. Chem. B, 2004, 108 (29), 10415-10427.
• Two-dimensional infrared measurements of the coupling between amide modes of an α-helix.  Chem. Phys. Lett., 2003, 382 (5-6), 586-592.