7b 2d 8 3d UPENN Biomedical Graduate Studies | Feng Gai 2 4c 2 19 2 9 8 2 13 2 2 14
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Feng Gai

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46 Contact information
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254 Chemistry 1973 Wing
38 231 South 34th Street
Philadelphia, PA 19104
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30 Office: (215) 573-6256
34 Fax: (215) 573-2112
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18 Publications
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13 Education:
21 a Ph.D. 1f (Physical Chemistry) c
34 Iowa State University, Ames, 1994.
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Description of Research Expertise

2bb The focus of our research is to study how proteins fold from random or quasi-random coils to their biologically functional conformations. We are particularly interested in the kinetic aspects of the folding mechanisms. Novel laser spectroscopic methods are being used and developed to study the early folding events and folding intermediates. Recent works involve the study of the helix-coil transition, helix-helix interaction, and â-sheet formation. In addition, single molecule techniques, such as confocal fluorescence spectroscopy and microscopy, are being used to investigate the heterogeneity in folding kinetics as well as protein spontaneous fluctuation and polymerization.
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Selected Publications

106 Z. Getahun, C-Y. Huang, T. Wang, B. D. León, W. F. DeGrado, and F. Gai: Using nitrile-derivatized amino acids as infrared probes of local environment. J. Am. Chem. Soc. 125: 405-411, 2003.

bc T. Wang, D. G. Du, and F. Gai: Helix-coil kinetics of two 14-residue peptides. Chem. Phys. Lett. 370: 842-48, 2003.

f7 C. Y. Huang, Z. Getahun, Y. J. Zhu, J. W. Klemke, W. F. DeGrado, and F. Gai: Helix formation via conformation diffusion search. Proc. Natl. Acad. Sci. USA 99: 2788-93, 2002.

df Y. Xu, R. Oyola, and F. Gai: Infrared study of the stability and folding kinetics of a 15-residue beta-hairpin. J. Am. Chem. Soc. 125: 15388-94, 2001.

fb C. Y. Huang, J. W. Klemke, Z. Getahun, W. F. DeGrado, and F. Gai: Temperature dependent helix-coil transition of an alanine based peptide. J. Am. Chem. Soc. 123: 9235-9238, 2001.

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