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Tel: 215-573-6256 |
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 β-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: Y. Xu, R. Oyola, and F. Gai
(2003) Infrared study of the stability and folding kinetics of a 15-residue
β-hairpin. J. Am. Chem. Soc. 125:15388-15394. Z. Getahun, C-Y. Huang, T.
Wang, B. D. León, W. F. DeGrado, and F. Gai (2003) Using nitrile-derivatized
amino acids as infrared probes of local environment. J. Am. Chem. Soc. 125:405-411. T. Wang, D. G. Du, and F. Gai
(2003) Helix-coil kinetics of two 14-residue peptides. Chem. Phys.
Lett. 370:842-848. C. Y. Huang, Z. Getahun, Y.
J. Zhu, J. W. Klemke, W. F. DeGrado, and F. Gai (2002) Helix formation
via conformation diffusion search. Proc. Natl. Acad. Sci. USA 99:2788-2793. C. Y. Huang, J. W. Klemke, Z. Getahun, W. F. DeGrado, and F. Gai (2001) Temperature dependent helix-coil transition of an alanine based peptide. J. Am. Chem. Soc. 123:9235-9238. |
