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10.1016/j.jmgm.2020.107778 http://scihub22266oqcxt.onion/10.1016/j.jmgm.2020.107778 33099199!7567490!33099199     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33099199&cmd=llinks): Failed to open stream: HTTP request failed! 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Exploring the intrinsic dynamics of SARS-CoV-2, SARS-CoV and MERS-CoV spike glycoprotein through normal mode analysis using anisotropic network model |pdf=|usr=}}{{33099199}} gab.com Text Exploring the intrinsic dynamics of SARS-CoV-2, SARS-CoV and MERS-CoV spike glycoprotein through normal mode analysis using anisotropic network model JO: J Mol Graph Model http://www.kidney.de/pget.php?&tw=1&pmid=33099199 #FOAvip COVID-19 caused by SARS-CoV-2 have become a global pandemic with serious rate of fatalities. SARS-CoV and MERS-CoV have also caused serious outbreak previously but the intensity was much lower than the ongoing SARS-CoV-2. The main infectivity factor of all the three viruses is the spike glycoprotein. In this study we have examined the intrinsic dynamics of the prefusion, lying state of trimeric S protein of these viruses through Normal Mode Analysis using Anisotropic Network Model. The dynamic modes of the S proteins of the aforementioned viruses were compared by root mean square inner product (RMSIP), spectral overlap and cosine correlation matrix. S proteins show homogenous correlated or anticorrelated motions among their domains but direction of C(alpha) atom among the spike proteins show less similarity. SARS-CoV-2 spike shows high vertically upward motion of the receptor binding motif implying its propensity for binding with the receptor even in the lying state. MERS-CoV spike shows unique dynamical motion compared to the other two S protein indicated by low RMSIP, spectral overlap and cosine correlation value. This study will guide in developing common potential inhibitor molecules against closed state of spike protein of these viruses to prevent conformational switching from lying to standing state. Twit Text FOAVip Exploring the intrinsic dynamics of SARS-CoV-2, SARS-CoV and MERS-CoV spike glycoprotein through normal mode analysis using anisotropic network model ????J Mol Graph Model http://www.kidney.de/pget.php?&tw=1&pmid=33099199 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33099199 #FOAvip English Wikipedia <ref>{{Cite pmid|33099199}}</ref> Exploring the intrinsic dynamics of SARS-CoV-2, SARS-CoV and MERS-CoV spike glycoprotein through normal mode analysis using anisotropic network model #MMPMID33099199 Majumder S; Chaudhuri D; Datta J; Giri K J Mol Graph Model 2021[Jan]; 102 (�): 107778 PMID33099199show ga COVID-19 caused by SARS-CoV-2 have become a global pandemic with serious rate of fatalities. SARS-CoV and MERS-CoV have also caused serious outbreak previously but the intensity was much lower than the ongoing SARS-CoV-2. The main infectivity factor of all the three viruses is the spike glycoprotein. In this study we have examined the intrinsic dynamics of the prefusion, lying state of trimeric S protein of these viruses through Normal Mode Analysis using Anisotropic Network Model. The dynamic modes of the S proteins of the aforementioned viruses were compared by root mean square inner product (RMSIP), spectral overlap and cosine correlation matrix. S proteins show homogenous correlated or anticorrelated motions among their domains but direction of C(alpha) atom among the spike proteins show less similarity. SARS-CoV-2 spike shows high vertically upward motion of the receptor binding motif implying its propensity for binding with the receptor even in the lying state. MERS-CoV spike shows unique dynamical motion compared to the other two S protein indicated by low RMSIP, spectral overlap and cosine correlation value. This study will guide in developing common potential inhibitor molecules against closed state of spike protein of these viruses to prevent conformational switching from lying to standing state. |COVID-19/virology[MESH] |Humans[MESH] |Middle East Respiratory Syndrome Coronavirus/*chemistry[MESH] |Models, Molecular[MESH] |Molecular Dynamics Simulation[MESH] |Pandemics[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |Protein Structure, Quaternary[MESH] |SARS-CoV-2/*chemistry[MESH] |Severe acute respiratory syndrome-related coronavirus/*chemistry[MESH]Exploring the intrinsic dynamics of SARS-CoV-2, SARS-CoV and MERS-CoV (epmc).pdf DeepDyve Pubget Overpricing