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10.1080/07391102.2020.1802338 http://scihub22266oqcxt.onion/10.1080/07391102.2020.1802338 32746720!7484573!32746720     free     free     free Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 249.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 249.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biomol+Struct+Dyn 2021 ; 39 (17): 6705-6712 Nephropedia Template TP {{tp|p=32746720|t=2021. Deciphering the protein motion of S1 subunit in SARS-CoV-2 spike glycoprotein through integrated computational methods |pdf=|usr=}}{{32746720}} gab.com Text Deciphering the protein motion of S1 subunit in SARS-CoV-2 spike glycoprotein through integrated computational methods JO: J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=32746720 #FOAvip The novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a major worldwide public health emergency that has infected over 8 million people. Spike glycoprotein, especially the partially open state of S1 subunit, in SARS-CoV-2 is considered vital for its infection with human host cell. However, the mechanism elucidating the transition from the closed state to the partially open state still remains unclear. In this study, we applied a series of computational methods, including Markov state model, transition path theory and random forest to analyze the S1 motion. Our results showed a promising complete conformational movement of the receptor-binding domain, from buried, partially open, to detached states. We also estimated the transition probability among these states. Based on the asymmetry in both the dynamics behavior and the accumulated alpha carbon (Calpha) importance, we further suggested a relation among chains in the trimer spike protein, which leads to a deeper understanding on protein motions of the S1 subunit.Communicated by Ramaswamy H. Sarma. Twit Text FOAVip Deciphering the protein motion of S1 subunit in SARS-CoV-2 spike glycoprotein through integrated computational methods ????J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=32746720 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32746720 #FOAvip English Wikipedia <ref>{{Cite pmid|32746720}}</ref> Deciphering the protein motion of S1 subunit in SARS-CoV-2 spike glycoprotein through integrated computational methods #MMPMID32746720 Tian H; Tao P J Biomol Struct Dyn 2021[Oct]; 39 (17): 6705-6712 PMID32746720show ga The novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a major worldwide public health emergency that has infected over 8 million people. Spike glycoprotein, especially the partially open state of S1 subunit, in SARS-CoV-2 is considered vital for its infection with human host cell. However, the mechanism elucidating the transition from the closed state to the partially open state still remains unclear. In this study, we applied a series of computational methods, including Markov state model, transition path theory and random forest to analyze the S1 motion. Our results showed a promising complete conformational movement of the receptor-binding domain, from buried, partially open, to detached states. We also estimated the transition probability among these states. Based on the asymmetry in both the dynamics behavior and the accumulated alpha carbon (Calpha) importance, we further suggested a relation among chains in the trimer spike protein, which leads to a deeper understanding on protein motions of the S1 subunit.Communicated by Ramaswamy H. Sarma. |*Spike Glycoprotein, Coronavirus/chemistry[MESH] |COVID-19/virology[MESH] |Computational Biology[MESH] |Humans[MESH] |Protein Binding[MESH]Deciphering the protein motion of S1 subunit in SARS-CoV-2 spike glyco(epmc).pdf DeepDyve Pubget Overpricing