Tanglab@PKU

Shangxiang Ye(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.

Chen Jingru (陈镜如)

E-mail: chenjingru@pku.edu.cn

Hi, I’m Chen Jingru, I completed my undergraduate study in physics at Central China Normal University, and now I am studying for a PhD at Peking University. Tanglab is a laboratory full of passion, creativity and love, I’m going to be a hot-wired, heat-seeking person, riding the wave, pushing the envelope in a sea of interdisciplinary subjects. I will make every effort to perform my duty, make my own contribution, and grow with Tanglab family side by side.

5月7—8日，以“强体魄，庆百年”为主题的北京大学第28届体育文化节暨2021年田径运动会在五四体育中心举行，全校万余名师生参加了本届运动会，运动会主要分为传统田径项目和趣味运动项目两部分。

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.

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.

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.

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.