Proper folding of proteins is essential for their biological functions. In contrast, misfolding and aggregation of proteins have been implicated in a wide array of diseases, such as Alzheimer’s disease and Type II Diabetes. The primary research endeavor of our group is directed to understand the underlying mechanisms of protein folding and misfolding. A multidisciplinary approach, integrating organic chemistry, protein engineering and biophysics, will be employed to probe the physio-chemical basis of protein folding/misfolding processes. Detailed understanding of protein folding mechanisms will provide guidelines for protein structure prediction and design of unnatural functional polymers. Knowledge on protein misfolding will enable us to understand the pathologies of protein misfolding diseases and foster novel therapeutic strategies for disease treatment.

Representative Key Publications:

Yanwen Fu, Jianmin Gao, Jan Bieschke, Maria, A. Dendle, and Jeffery W. Kelly, “Amide-to-E-Olefin versus Amide-to-Ester Backbone H-Bond Perturbations: Evaluating the Repulsive Lone Pair-Lone Pair interaction for Extracting H-Bond Energies.” J. Am. Chem. Soc. 2006, 128, 15948-15949.

Jianmin Gao, Haibo Liu, and Eric T. Kool, “Assembly of the Complete Eight-Base Artificial Genetic Helix, xDNA, and Its Interaction with the Natural Genetic System” Angew. Chem. Int. Ed. 2005, 44, 3118-3122.

Jianmin Gao, Soichiro Watanabe, and Eric T. Kool, “Modified DNA Analogues That Sense Light Exposure with Color Changes”, J. Am. Chem. Soc., 2004, 126, 12748-12749.