Our research interests lie in the interface between biology and other areas of science (chemistry and physics). NMR is our primary tool for structural and biophysical analysis. We also extensively use other techniques including Circular Dichroism and Fluorescence spectroscopy, and Isothermal calorimetry. These biophysical analyses are corroborated by sophisticated engineering and tuning of target proteins using semi-synthetic chemical biology techniques, in addition to traditional molecular biology methods.
- Ph.D. in , Stony Brook University - (Stony Brook, New York, United States) 2006
- M.S. in Protein Engineering, Pohang University of Science and Technology - (Pohang, South Korea) 1999
- B.S. in Biology, Hanyang University - (Seoul, South Korea) 1997
- Shen, Q., & Cho, J. (2019). The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus. Biochem Biophys Res Commun. 518(1), 178-182.
- Shen, Q., Shi, J., Zeng, D., Zhao, B., Li, P., Hwang, W., & Cho, J. (2018). Molecular Mechanisms of Tight Binding through Fuzzy Interactions. Biophys J. 114(6), 1313-1320.
- Shen, Q., Bhatt, V. S., Krieger, I., Sacchettini, J. C., & Cho, J. (2018). Structure-guided design of a potent peptide inhibitor targeting the interaction between CRK and ABL kinase. MEDCHEMCOMM. 9(3), 519-524.
- Shen, Q., Zeng, D., Zhao, B., Bhatt, V. S., Li, P., & Cho, J. (2017). The Molecular Mechanisms Underlying the Hijack of Host Proteins by the 1918 Spanish Influenza Virus. ACS Chemical Biology. 12(5), 1199-1203.
- Sato, S., Cho, J., Peran, I., Soydaner-Azeloglu, R. G., & Raleigh, D. P. (2017). The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State. Biophys J. 112(9), 1797-1806.