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10.1016/j.bpj.2021.01.012 http://scihub22266oqcxt.onion/10.1016/j.bpj.2021.01.012 33484712!7825899!33484712     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+J 2021 ; 120 (6): 1060-1071 Nephropedia Template TP {{tp|p=33484712|t=2021. Elucidation of interactions regulating conformational stability and dynamics of SARS-CoV-2 S-protein |pdf=|usr=}}{{33484712}} gab.com Text Elucidation of interactions regulating conformational stability and dynamics of SARS-CoV-2 S-protein JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=33484712 #FOAvip The ongoing COVID-19 pandemic caused by the new coronavirus, SARS-CoV-2, calls for urgent developments of vaccines and antiviral drugs. The spike protein of SARS-CoV-2 (S-protein), which consists of trimeric polypeptide chains with glycosylated residues on the surface, triggers the virus entry into a host cell. Extensive structural and functional studies on this protein have rapidly advanced our understanding of the S-protein structure at atomic resolutions, although most of these structural studies overlook the effect of glycans attached to the S-protein on the conformational stability and functional motions between the inactive down and active up forms. Here, we performed all-atom molecular dynamics simulations of both down and up forms of a fully glycosylated S-protein in solution as well as targeted molecular dynamics simulations between them to elucidate key interdomain interactions for stabilizing each form and inducing the large-scale conformational transitions. The residue-level interaction analysis of the simulation trajectories detects distinct amino acid residues and N-glycans as determinants on conformational stability of each form. During the conformational transitions between them, interdomain interactions mediated by glycosylated residues are switched to play key roles on the stabilization of another form. Electrostatic interactions, as well as hydrogen bonds between the three receptor binding domains, work as driving forces to initiate the conformational transitions toward the active form. This study sheds light on the mechanisms underlying conformational stability and functional motions of the S-protein, which are relevant for vaccine and antiviral drug developments. Twit Text FOAVip Elucidation of interactions regulating conformational stability and dynamics of SARS-CoV-2 S-protein ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=33484712 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33484712 #FOAvip English Wikipedia <ref>{{Cite pmid|33484712}}</ref> Elucidation of interactions regulating conformational stability and dynamics of SARS-CoV-2 S-protein #MMPMID33484712 Mori T; Jung J; Kobayashi C; Dokainish HM; Re S; Sugita Y Biophys J 2021[Mar]; 120 (6): 1060-1071 PMID33484712show ga The ongoing COVID-19 pandemic caused by the new coronavirus, SARS-CoV-2, calls for urgent developments of vaccines and antiviral drugs. The spike protein of SARS-CoV-2 (S-protein), which consists of trimeric polypeptide chains with glycosylated residues on the surface, triggers the virus entry into a host cell. Extensive structural and functional studies on this protein have rapidly advanced our understanding of the S-protein structure at atomic resolutions, although most of these structural studies overlook the effect of glycans attached to the S-protein on the conformational stability and functional motions between the inactive down and active up forms. Here, we performed all-atom molecular dynamics simulations of both down and up forms of a fully glycosylated S-protein in solution as well as targeted molecular dynamics simulations between them to elucidate key interdomain interactions for stabilizing each form and inducing the large-scale conformational transitions. The residue-level interaction analysis of the simulation trajectories detects distinct amino acid residues and N-glycans as determinants on conformational stability of each form. During the conformational transitions between them, interdomain interactions mediated by glycosylated residues are switched to play key roles on the stabilization of another form. Electrostatic interactions, as well as hydrogen bonds between the three receptor binding domains, work as driving forces to initiate the conformational transitions toward the active form. This study sheds light on the mechanisms underlying conformational stability and functional motions of the S-protein, which are relevant for vaccine and antiviral drug developments. |*Molecular Dynamics Simulation[MESH] |Hydrogen Bonding[MESH] |Polysaccharides/metabolism[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |Protein Stability[MESH] |Solutions[MESH] |Spike Glycoprotein, Coronavirus/*chemistry[MESH]Elucidation of interactions regulating conformational stability and dy(epmc).pdf DeepDyve Pubget Overpricing