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Jianhan Chen Computational Biochemistry & Biophysics B.S. 1998, University of Science and Technology of China Our general focus is on theoretical and computational studies of biomolecular structure, dynamics and function. We are particularly interested in modeling weakly stable peptides and proteins and understanding their roles in important biological processes including regulation of transcription and translation, signal transduction and disease-related protein misfolding. In collaboration with John Tomich's lab, we also apply computer modeling to determine the selectivity, transport and gating mechanisms of designed anion selective channels. Please visit our lab web page for more up-to-date information. |
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785-532-2518 |
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Selected Publications: W. Zhang, D. Ganguly and J. Chen (2012). "Residual Structures, Conformational Fluctuations, and Electrostatic Interactions in the Synergistic Folding of Two Intrinsically Disordered Proteins" PLoS Comput. Biol. (in press) U. Bukovnik, J. Gao, J., G.A. Cook1, L.P. Shank, M.B. Seabra, B.D. Schultz, T. Iwamoto, J. Chen and J.M. Tomich (2012). "Structural and biophysical properties of a synthetic channel-forming peptide: Designing a clinically relevant anion selective pore", BBA - Biomembranes (in press) D. Ganguly, W. Zhang and J. Chen (2012). "Synergetic folding of two intrinsically disordered proteins. Searching for conformational selection", Mol. BioSys. 8, 198-209. (Front Cover) J. Chen and A. Zolkiewska (2011). "Force-Induced Unfolding Simulation of the Human Notch1 Negative Regulatory Region: Possible Roles of the Heterodimerization Domain in Mechanosensing", PLoS ONE 6(7): e22837. Y. Wang, J. C. Fisher, R. Matthew, L. Ou, S. Otieno, J. Sublett, L. Xiao, J. Chen, M. F. Roussel, and R. W. Kriwacki (2011). "Intrinsic Disorder Mediates the Diverse Cell Cycle Regulatory Functions of the Cyclin-dependent Kinase Inhibitor, p21Cip1", Nature Chem. Biol. 7, 214-221. D. Ganguly and J. Chen (2011). "Topology-based modeling of intrinsically disordered proteins: balancing intrinsic structural propensities and intermolecular interactions", PROTEINS 79, 1251-1266. |