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10.1116/6.0000502 http://scihub22266oqcxt.onion/10.1116/6.0000502 33105999!ä!33105999 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biointerphases 2020 ; 15 (5): 051008 Nephropedia Template TP {{tp|p=33105999|t=2020. Computer simulations of the interaction between SARS-CoV-2 spike glycoprotein and different surfaces |pdf=|usr=}}{{33105999}} gab.com Text Computer simulations of the interaction between SARS-CoV-2 spike glycoprotein and different surfaces JO: Biointerphases http://www.kidney.de/pget.php?&tw=1&pmid=33105999 #FOAvip A prominent feature of coronaviruses is the presence of a large glycoprotein spike protruding from a lipidic membrane. This glycoprotein spike determines the interaction of coronaviruses with the environment and the host. In this paper, we perform all atomic molecular dynamics simulations of the interaction between the SARS-CoV-2 trimeric glycoprotein spike and surfaces of materials. We considered a material with high hydrogen bonding capacity (cellulose) and a material capable of strong hydrophobic interactions (graphite). Initially, the spike adsorbs to both surfaces through essentially the same residues belonging to the receptor binding subunit of its three monomers. Adsorption onto cellulose stabilizes in this configuration, with the help of a large number of hydrogen bonds developed between cellulose and the three receptor-binding domains of the glycoprotein spike. In the case of adsorption onto graphite, the initial adsorption configuration is not stable and the surface induces a substantial deformation of the glycoprotein spike with a large number of adsorbed residues not pertaining to the binding subunits of the spike monomers. Twit Text FOAVip Computer simulations of the interaction between SARS-CoV-2 spike glycoprotein and different surfaces ????Biointerphases http://www.kidney.de/pget.php?&tw=1&pmid=33105999 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33105999 #FOAvip English Wikipedia <ref>{{Cite pmid|33105999}}</ref> Computer simulations of the interaction between SARS-CoV-2 spike glycoprotein and different surfaces #MMPMID33105999 Malaspina DC; Faraudo J Biointerphases 2020[Oct]; 15 (5): 051008 PMID33105999show ga A prominent feature of coronaviruses is the presence of a large glycoprotein spike protruding from a lipidic membrane. This glycoprotein spike determines the interaction of coronaviruses with the environment and the host. In this paper, we perform all atomic molecular dynamics simulations of the interaction between the SARS-CoV-2 trimeric glycoprotein spike and surfaces of materials. We considered a material with high hydrogen bonding capacity (cellulose) and a material capable of strong hydrophobic interactions (graphite). Initially, the spike adsorbs to both surfaces through essentially the same residues belonging to the receptor binding subunit of its three monomers. Adsorption onto cellulose stabilizes in this configuration, with the help of a large number of hydrogen bonds developed between cellulose and the three receptor-binding domains of the glycoprotein spike. In the case of adsorption onto graphite, the initial adsorption configuration is not stable and the surface induces a substantial deformation of the glycoprotein spike with a large number of adsorbed residues not pertaining to the binding subunits of the spike monomers. |Adsorption[MESH] |Betacoronavirus/isolation & purification/*metabolism[MESH] |Binding Sites[MESH] |COVID-19[MESH] |Cellulose/chemistry/metabolism[MESH] |Coronavirus Infections/pathology/virology[MESH] |Graphite/chemistry/metabolism[MESH] |Humans[MESH] |Hydrogen Bonding[MESH] |Hydrophobic and Hydrophilic Interactions[MESH] |Molecular Dynamics Simulation[MESH] |Pandemics[MESH] |Pneumonia, Viral/pathology/virology[MESH] |Protein Binding[MESH] |SARS-CoV-2[MESH] |Spike Glycoprotein, Coronavirus/chemistry/*metabolism[MESH]Computer simulations of the interaction between SARS-CoV-2 spike glyco(epmc).pdf DeepDyve Pubget Overpricing