changwen jin

The research of Professor Jin’s group exploits the potential of Nuclear Magnetic Resonance (NMR) techniques for the study of the structures, dynamics and biological functions of proteins, especially enzymes. In particular, they are interested in the correlation between protein dynamics (structural fluctuations over time) and their functional mechanisms. Further, they investigate the interactions of protein with other molecules, for instance, receptor-ligand and enzyme-substrate, as well as protein-protein interactions. The Jin Group uses novel NMR methods like PRE, RDC, CEST and CPMG RD, and in parallel they uses biochemical methods to characterize the activity and functions of proteins both in vitro and in vivo. The group’s main goal is to elucidate the structural and dynamic basis of protein functions.

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Peking University

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NMR Technologies 0 Protein Structures and Dynamics 0 Protein Interactions 0 Membrane proteins 0

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  1. Niu X, Ma S, Hu Y, Jin C. Backbone 1H, 13C and 15N resonance assignments of the proteasome lid subunit Rpn12 from Saccharomyces cerevisiae. Biomol NMR Assign. 2020;14(1):147-150. doi:10.1007/s12104-020-09935-w

  2. Xu J, Hu Y, Kaindl J, et al. Conformational Complexity and Dynamics in a Muscarinic Receptor Revealed by NMR Spectroscopy. Mol Cell. 2019;75(1):53-65.e7. doi:10.1016/j.molcel.2019.04.028

  3. Jia M, Hu Y, Jin C. 1H, 13C and 15N resonance assignments of the second peptidyl-prolyl isomerase domain of chaperone SurA from Escherichia coli. Biomol NMR Assign. 2019;13(1):183-186. doi:10.1007/s12104-019-09874-1

  4. Yu XC, Hu Y, Ding J, Li H, Jin C. Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone. J Biol Chem. 2019;294(9):3192-3206. doi:10.1074/jbc.RA118.006398

  5. Zhang W, Zhao C, Hu Y, Jin C. NMR 1H, 13C, 15N backbone and side chain resonance assignment of the N-terminal domain of yeast proteasome lid subunit Rpn5. Biomol NMR Assign. 2019;13(1):1-4. doi:10.1007/s12104-018-9840-5


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