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10.1002/jcc.26383 http://scihub22266oqcxt.onion/10.1002/jcc.26383 32779780!7404873!32779780     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Comput+Chem 2020 ; 41 (24): 2158-2161 Nephropedia Template TP {{tp|p=32779780|t=2020. Atomistic simulation reveals structural mechanisms underlying D614G spike glycoprotein-enhanced fitness in SARS-COV-2 |pdf=|usr=}}{{32779780}} gab.com Text Atomistic simulation reveals structural mechanisms underlying D614G spike glycoprotein-enhanced fitness in SARS-COV-2 JO: J Comput Chem http://www.kidney.de/pget.php?&tw=1&pmid=32779780 #FOAvip D614G spike glycoprotein (sgp) mutation in rapidly spreading severe acute respiratory syndrome coronavirus-2 (SARS-COV-2) is associated with enhanced fitness and higher transmissibility in new cases of COVID-19 but the underlying mechanism is unknown. Here, using atomistic simulation, a plausible mechanism has been delineated. In G614 sgp but not wild type, increased D(G)614-T859 Calpha-distance within 65 ns is interpreted as S1/S2 protomer dissociation. Overall, ACE2-binding, post-fusion core, open-state and sub-optimal antibody-binding conformations were preferentially sampled by the G614 mutant, but not wild type. Furthermore, in the wild type, only one of the three sgp chains has optimal communication route between residue 614 and the receptor-binding domain (RBD); whereas, two of the three chains communicated directly in G614 mutant. These data provide evidence that D614G sgp mutant is more available for receptor binding, cellular invasion and reduced antibody interaction; thus, providing framework for enhanced fitness and higher transmissibility in D614G SARS-COV-2 mutant. Twit Text FOAVip Atomistic simulation reveals structural mechanisms underlying D614G spike glycoprotein-enhanced fitness in SARS-COV-2 ????J Comput Chem http://www.kidney.de/pget.php?&tw=1&pmid=32779780 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32779780 #FOAvip English Wikipedia <ref>{{Cite pmid|32779780}}</ref> Atomistic simulation reveals structural mechanisms underlying D614G spike glycoprotein-enhanced fitness in SARS-COV-2 #MMPMID32779780 Omotuyi IO; Nash O; Ajiboye OB; Iwegbulam CG; Oyinloye EB; Oyedeji OA; Kashim ZA; Okaiyeto K J Comput Chem 2020[Sep]; 41 (24): 2158-2161 PMID32779780show ga D614G spike glycoprotein (sgp) mutation in rapidly spreading severe acute respiratory syndrome coronavirus-2 (SARS-COV-2) is associated with enhanced fitness and higher transmissibility in new cases of COVID-19 but the underlying mechanism is unknown. Here, using atomistic simulation, a plausible mechanism has been delineated. In G614 sgp but not wild type, increased D(G)614-T859 Calpha-distance within 65 ns is interpreted as S1/S2 protomer dissociation. Overall, ACE2-binding, post-fusion core, open-state and sub-optimal antibody-binding conformations were preferentially sampled by the G614 mutant, but not wild type. Furthermore, in the wild type, only one of the three sgp chains has optimal communication route between residue 614 and the receptor-binding domain (RBD); whereas, two of the three chains communicated directly in G614 mutant. These data provide evidence that D614G sgp mutant is more available for receptor binding, cellular invasion and reduced antibody interaction; thus, providing framework for enhanced fitness and higher transmissibility in D614G SARS-COV-2 mutant. |*Computer Simulation[MESH] |*Models, Chemical[MESH] |Amino Acid Sequence[MESH] |Betacoronavirus/*metabolism[MESH] |Binding Sites[MESH] |COVID-19[MESH] |Coronavirus Infections/*virology[MESH] |Humans[MESH] |Models, Molecular[MESH] |Mutation[MESH] |Pandemics[MESH] |Pneumonia, Viral/*virology[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |SARS-CoV-2[MESH]Atomistic simulation reveals structural mechanisms underlying D614G sp(epmc).pdf DeepDyve Pubget Overpricing