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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.


biomolecular_dynamics_study(before 2021)


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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