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10.1021/acs.nanolett.0c04465

http://scihub22266oqcxt.onion/10.1021/acs.nanolett.0c04465
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suck abstract from ncbi


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pmid33474931      Nano+Lett 2021 ; 21 (6): 2675-2680
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  • Topography, Spike Dynamics, and Nanomechanics of Individual Native SARS-CoV-2 Virions #MMPMID33474931
  • Kiss B; Kis Z; Palyi B; Kellermayer MSZ
  • Nano Lett 2021[Mar]; 21 (6): 2675-2680 PMID33474931show ga
  • SARS-CoV-2, the virus responsible for the current COVID-19 pandemic, displays a corona-shaped layer of spikes which play a fundamental role in the infection process. Recent structural data suggest that the spikes possess orientational freedom and the ribonucleoproteins segregate into basketlike structures. How these structural features regulate the dynamic and mechanical behavior of the native virion are yet unknown. By imaging and mechanically manipulating individual, native SARS-CoV-2 virions with atomic force microscopy, here, we show that their surface displays a dynamic brush owing to the flexibility and rapid motion of the spikes. The virions are highly compliant and able to recover from drastic mechanical perturbations. Their global structure is remarkably temperature resistant, but the virion surface becomes progressively denuded of spikes upon thermal exposure. The dynamics and the mechanics of SARS-CoV-2 are likely to affect its stability and interactions.
  • |Biomechanical Phenomena[MESH]
  • |COVID-19/*virology[MESH]
  • |Hot Temperature[MESH]
  • |Humans[MESH]
  • |Microscopy, Atomic Force[MESH]
  • |Models, Molecular[MESH]
  • |Nanostructures/chemistry/ultrastructure[MESH]
  • |Nanotechnology[MESH]
  • |Pandemics[MESH]
  • |Protein Conformation[MESH]
  • |Protein Stability[MESH]
  • |SARS-CoV-2/*chemistry/*physiology/ultrastructure[MESH]
  • |Single Molecule Imaging[MESH]
  • |Spike Glycoprotein, Coronavirus/*chemistry/*physiology/ultrastructure[MESH]
  • |Thermodynamics[MESH]


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