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10.1089/cmb.2020.0193 http://scihub22266oqcxt.onion/10.1089/cmb.2020.0193 32401043!ä!32401043 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\32401043.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Comput+Biol 2020 ; 27 (11): 1622-1630 Nephropedia Template TP {{tp|p=32401043|t=2020. Conserved High Free Energy Sites in Human Coronavirus Spike Glycoprotein Backbones |pdf=|usr=}}{{32401043}} gab.com Text Conserved High Free Energy Sites in Human Coronavirus Spike Glycoprotein Backbones JO: J Comput Biol http://www.kidney.de/pget.php?&tw=1&pmid=32401043 #FOAvip 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. Twit Text FOAVip Conserved High Free Energy Sites in Human Coronavirus Spike Glycoprotein Backbones ????J Comput Biol http://www.kidney.de/pget.php?&tw=1&pmid=32401043 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32401043 #FOAvip English Wikipedia <ref>{{Cite pmid|32401043}}</ref> 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]Conserved High Free Energy Sites in Human Coronavirus Spike Glycoprote(epmc).pdf DeepDyve Pubget Overpricing