TangLab in College of Chemistry and Molecular Engineering & Center for Life Sciences @Peking University focus on Biomolecular Dynamics, etc...

Publications

Publications

76 Jian-Hua Wang, Yu-Liang Tang, Zhou Gong, Rohit Jain, Fan Xiao, Yu Zhou, Dan Tan, Qiang Li, Niu Huang, Shu-Qun Liu, Keqiong Ye, Chun Tang, Meng-Qiu Dong & Xiaoguang Lei, “Characterization of protein unfolding by fast cross-linking mass spectrometry using di-ortho-phthalaldehyde cross-linkers” Nat Commun 13, 1468 (2022). https://doi.org/10.1038/s41467-022-28879-4

75 Yingxue Ma, Haozheng Li, Zhou Gong, Shuai Yang, Ping Wang, and Chun Tang, 2022,”Nucleobase Clustering Contributes to the Formation and Hollowing of Repeat-Expansion RNA Condensate” J. Am. Chem. Soc. https://doi.org/10.1021/jacs.1c12085

74 Xu Dong, Ling-Yun Qin, Zhou Gong, Sanbo Qin, Huan-Xiang Zhou, and Chun Tang,2022.”Preferential Interactions of a Crowder Protein with the Specific Binding Site of a Native Protein Complex” J. Phys. Chem. Lett.: 792–800https://doi.org/10.1021/acs.jpclett.1c03794

73 Czaplewski, C., et al. (2021). “Recent Developments in Data-Assisted Modeling of Flexible Proteins.” Frontiers in Molecular Biosciences 8(1306).https://doi.org/10.3389/fmolb.2021.765562

72 Fu, W., et al. (2021). “Discovery of a Novel Androgen Receptor Antagonist Manifesting Evidence to Disrupt the Dimerization of the Ligand-Binding Domain via Attenuating the Hydrogen-Bonding Network Between the Two Monomers.” Journal of Medicinal Chemistry 64(23): 17221-17238.https://doi.org/10.1021/acs.jmedchem.1c01287

71 Kogut M, Gong Z, Tang C, Liwo A. (2021) Pseudopotentials for coarse‐grained cross‐link‐assisted modeling of protein structures
M Kogut, Z Gong, C Tang, A Liwo Journal of Computational Chemistry 42 (29), 2054-2067 Journal of Computational Chemistry, doi.org/10.1002/jcc.26736

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Phd Students

Shangxiang Ye(叶尚祥)

叶尚祥

Email: yeshangxiang@wipm.ac.cn

Hi, I am Shangxiang Ye. I obtained my Bachelor degree from Central China Normal University Now I am studying for a PhD in Tang lab. It’s my pleasure to be a member of Tang lab. And my main research work is to study the molecular mechanism of PINK1/Parkin-mediated mitophagy.

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Undergrad

Haoyang Deng(邓皓洋)

邓皓洋

E-mail: denghaoyang@pku.edu.cn

I am Haoyang Deng. I am studying in College of Molecular Engineering, Peking University, and I will be major in chemical biology. Now I am working in Tang Lab for undergraduate research.

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PRE

Lanthanoid tagging via an unnatural amino acid for protein structure characterization

Lanthanoid pseudo-contact shift (PCS) provides long-range structural information between a paramagnetic tag and protein nuclei. Here we report two lanthanoid probes, DTTA-C3-yne and DTTA-C4-yne, which can be conjugated to an unnatural amino acid pAzF in the target protein via azide-alkyne cycloaddition. The DTTA-based lanthanoid tags are associated with large magnetic susceptibility tensors owing to the rigidity of the tags.

Reference: J Biomol NMR, 2017, 67:273-282.

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RNA

Conjoined use of EM and NMR in RNA structure refinement

Hence structural characterization of large RNAs can be difficult for NMR alone. Electron microscopy (EM) provides global shape information of macromolecules at nanometer resolution, which should be complementary to NMR for RNA structure determination.

Reference: Plos One, 2015,10, e0120445.

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UB

Integration of smFRET and NMR to study the dynamic structure and function of K48-linked ubiquitin chain

K48 linked ubiquitin chains can mediate the degradation of substrate protein by Proteasome. This study uses NMR as the main method to analyze the solution structure of K48-diUb:Rpn13NTD, In addition, using smFRET we proved that Rpn13 specifically binds to the closed state of the K48 linked ubiquitin chains through conformational selection. This work provides the structural baisis for Rpn13 linkage selectivity, which opens a new window for modulating proteasomal function.

Reference: Cell Discov, 2019, 5:9.

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biomolecular_dynamics_study(before 2021)

CXMS

Chemical cross-linking coupled with mass spectroscopy (CXMS) provides proximity information for the cross-linked residues. Protein dynamics can be manifested from cross-links, as illustrated here with the open-closed domain movement for a two-domain protein.

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