Jae-hyun Cho
professor
Biochemistry and Biophysics
Texas A and M University
United States of America
Biography
Hyun cho explained the importance of understanding the regulatory mechanism of the intra-molecular interactions is highlighted by the observation that nearly 65%-80% of eukaryotic proteins consist of multiple domains. The multidomain architecture generates “emergent properties” that are not demonstrated by their individual domains and should be investigated in the context of full-length protein. In these systems, the dynamics of the intra-molecular interactions between domains provides fundamental mechanisms for many biological processes such as autoinhibition, allosteric modulation of kinase activity and molecular recognition of target proteins.
Research Interest
His 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.
Publications
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Zeng, D, Shen, Q, Cho, JH. Thermodynamic contribution of backbone conformational entropy in the binding between SH3 domain and proline-rich motif. Biochem. Biophys. Res. Commun. 2017;484 (1):21-26. doi: 10.1016/j.bbrc.2017.01.089. PubMed PMID:28111343. .
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Shen, Q, Zeng, D, Zhao, B, Bhatt, VS, Li, P, Cho, JH et al.. The Molecular Mechanisms Underlying the Hijack of Host Proteins by the 1918 Spanish Influenza Virus. ACS Chem. Biol. 2017;12 (5):1199-1203. doi: 10.1021/acschembio.7b00168. PubMed PMID:28368102. .
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Sato, S, Cho, JH, Peran, I, Soydaner-Azeloglu, RG, Raleigh, DP. The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State. Biophys. J. 2017;112 (9):1797-1806. doi: 10.1016/j.bpj.2017.01.034. PubMed PMID:28494951. PubMed Central PMC5425357.
