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10.1039/d0sc05330a

http://scihub22266oqcxt.onion/10.1039/d0sc05330a
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34163908!8179027!34163908
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suck abstract from ncbi


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pmid34163908      Chem+Sci 2020 ; 12 (4): 1451-1457
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  • Probing conformational hotspots for the recognition and intervention of protein complexes by lysine reactivity profiling #MMPMID34163908
  • Liu Z; Zhang W; Sun B; Ma Y; He M; Pan Y; Wang F
  • Chem Sci 2020[Nov]; 12 (4): 1451-1457 PMID34163908show ga
  • Probing the conformational and functional hotspot sites within aqueous native protein complexes is still a challenging task. Herein, a mass spectrometry (MS)-based two-step isotope labeling-lysine reactivity profiling (TILLRP) strategy is developed to quantify the reactivities of lysine residues and probe the molecular details of protein-protein interactions as well as evaluate the conformational interventions by small-molecule active compounds. The hotspot lysine sites that are crucial to the SARS-CoV-2 S1-ACE2 combination could be successfully probed, such as S1 Lys(417) and Lys(444). Significant alteration of the reactivities of lysine residues at the interaction interface of S1-RBD Lys(386)-Lys(462) was observed during the formation of complexes, which might be utilized as indicators for investigating the S1-ACE2 dynamic recognition and intervention at the molecular level in high throughput.
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