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10.1089/cmb.2020.0193

http://scihub22266oqcxt.onion/10.1089/cmb.2020.0193
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32401043!ä!32401043

suck abstract from ncbi


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pmid32401043      J+Comput+Biol 2020 ; 27 (11): 1622-1630
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  • Conserved High Free Energy Sites in Human Coronavirus Spike Glycoprotein Backbones #MMPMID32401043
  • Penner RC
  • J Comput Biol 2020[Nov]; 27 (11): 1622-1630 PMID32401043show ga
  • Methods previously developed by the author are applied to uncover several sites of interest in the spike glycoproteins of all known human coronaviruses (hCoVs), including SARS-CoV-2 that causes COVID-19. The sites comprise three-dimensional neighborhoods of peptides characterized by four key properties: (1) they pinpoint regions of high free energy in the backbone whose obstruction might interrupt function; (2) by their very definition, they occur rarely in the universe of all gene-encoded proteins that could obviate host response to compounds designed for their interference; (3) they are common to all known hCoV spikes, possibly retaining activity in light of inevitable viral mutation; and (4) they are exposed in the molecular surface of the glycoprotein. These peptides in SARS-CoV-2 are given by the triples of residues (131, 117, 134), (203, 227, 228), and (1058, 730, 731) in its spike.
  • |Betacoronavirus/chemistry[MESH]
  • |COVID-19[MESH]
  • |Coronavirus Infections/*virology[MESH]
  • |Coronavirus/*chemistry[MESH]
  • |Databases, Protein[MESH]
  • |Humans[MESH]
  • |Hydrogen Bonding[MESH]
  • |Models, Molecular[MESH]
  • |Pandemics[MESH]
  • |Pneumonia, Viral/virology[MESH]
  • |Protein Conformation[MESH]
  • |SARS-CoV-2[MESH]
  • |Spike Glycoprotein, Coronavirus/*chemistry[MESH]


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