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兴大报告学术笔记—Ichio Shimada 教授

应北京大学化学学院唐淳教授的邀请,RIKEN BDR生物分子动态结构实验室的组长,著名学者Ichio Shimada 教授,于2021年10月29日下午,在线上为北京大学的师生们做了题为“Function-Related Dynamics of Membrane Proteins by NMR”的兴大报告。

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Tanglab庆祝2021教师节

为庆祝2021年教师节的到来,Tanglab的成员为唐老师进行准备了颈椎按摩器。

颈椎按摩器对长期伏案工作的人员有很好的按摩作用,可以放松神经、血管与颈部肌肉。之后,唐老师邀请实验室成员体验了按摩器,体验了被电的酥酥麻麻的滋味。

20210910-Tanglab@PKU合照

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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