Feng Gai

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Graduate Group Affiliations

Contact information
254 Chemistry 1973 Wing
231 South 34th Street
Philadelphia, PA 19104
Office: (215) 573-6256
Fax: (215) 573-2112
Ph.D. (Physical Chemistry)
Iowa State University, Ames, 1994.
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Description of Research Expertise

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.

Selected Publications

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.

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

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.

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.

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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Last updated: 08/25/2004
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