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10.1063/5.0011141 http://scihub22266oqcxt.onion/10.1063/5.0011141 32828084!ä!32828084 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Chem+Phys 2020 ; 153 (7): 075101 Nephropedia Template TP {{tp|p=32828084|t=2020. Conformational transition of SARS-CoV-2 spike glycoprotein between its closed and open states |pdf=|usr=}}{{32828084}} gab.com Text Conformational transition of SARS-CoV-2 spike glycoprotein between its closed and open states JO: J Chem Phys http://www.kidney.de/pget.php?&tw=1&pmid=32828084 #FOAvip In 2020, the novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has infected millions of people worldwide and caused the coronavirus disease 2019 (COVID-19). Spike (S) glycoproteins on the viral membrane bind to ACE2 receptors on the host cell membrane and initiate fusion, and S protein is currently among the primary drug target to inhibit viral entry. The S protein can be in a receptor inaccessible (closed) or accessible (open) state based on down and up positions of its receptor-binding domain (RBD), respectively. However, conformational dynamics and the transition pathway between closed to open states remain unexplored. Here, we performed all-atom molecular dynamics (MD) simulations starting from closed and open states of the S protein trimer in the presence of explicit water and ions. MD simulations showed that RBD forms a higher number of interdomain interactions and exhibits lower mobility in its down position than its up position. MD simulations starting from intermediate conformations between the open and closed states indicated that RBD switches to the up position through a semi-open intermediate that potentially reduces the free energy barrier between the closed and open states. Free energy landscapes were constructed, and a minimum energy pathway connecting the closed and open states was proposed. Because RBD-ACE2 binding is compatible with the semi-open state, but not with the closed state of the S protein, we propose that the formation of the intermediate state is a prerequisite for the host cell recognition. Twit Text FOAVip Conformational transition of SARS-CoV-2 spike glycoprotein between its closed and open states ????J Chem Phys http://www.kidney.de/pget.php?&tw=1&pmid=32828084 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32828084 #FOAvip English Wikipedia <ref>{{Cite pmid|32828084}}</ref> Conformational transition of SARS-CoV-2 spike glycoprotein between its closed and open states #MMPMID32828084 Gur M; Taka E; Yilmaz SZ; Kilinc C; Aktas U; Golcuk M J Chem Phys 2020[Aug]; 153 (7): 075101 PMID32828084show ga In 2020, the novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has infected millions of people worldwide and caused the coronavirus disease 2019 (COVID-19). Spike (S) glycoproteins on the viral membrane bind to ACE2 receptors on the host cell membrane and initiate fusion, and S protein is currently among the primary drug target to inhibit viral entry. The S protein can be in a receptor inaccessible (closed) or accessible (open) state based on down and up positions of its receptor-binding domain (RBD), respectively. However, conformational dynamics and the transition pathway between closed to open states remain unexplored. Here, we performed all-atom molecular dynamics (MD) simulations starting from closed and open states of the S protein trimer in the presence of explicit water and ions. MD simulations showed that RBD forms a higher number of interdomain interactions and exhibits lower mobility in its down position than its up position. MD simulations starting from intermediate conformations between the open and closed states indicated that RBD switches to the up position through a semi-open intermediate that potentially reduces the free energy barrier between the closed and open states. Free energy landscapes were constructed, and a minimum energy pathway connecting the closed and open states was proposed. Because RBD-ACE2 binding is compatible with the semi-open state, but not with the closed state of the S protein, we propose that the formation of the intermediate state is a prerequisite for the host cell recognition. |Angiotensin-Converting Enzyme 2[MESH] |Betacoronavirus/*chemistry[MESH] |Binding Sites[MESH] |Hydrogen Bonding[MESH] |Models, Chemical[MESH] |Molecular Dynamics Simulation[MESH] |Peptidyl-Dipeptidase A/chemistry/metabolism[MESH] |Principal Component Analysis[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |Receptors, Virus/chemistry/metabolism[MESH] |SARS-CoV-2[MESH] |Spike Glycoprotein, Coronavirus/*chemistry/metabolism[MESH]Conformational transition of SARS-CoV-2 spike glycoprotein between its(epmc).pdf DeepDyve Pubget Overpricing