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10.1016/j.virol.2021.06.009 http://scihub22266oqcxt.onion/10.1016/j.virol.2021.06.009 34217923!8237243!34217923     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Virology 2021 ; 561 (ä): 107-116 Nephropedia Template TP {{tp|p=34217923|t=2021. Insilico study on the effect of SARS-CoV-2 RBD hotspot mutants interaction with ACE2 to understand the binding affinity and stability |pdf=|usr=}}{{34217923}} gab.com Text Insilico study on the effect of SARS-CoV-2 RBD hotspot mutants interaction with ACE2 to understand the binding affinity and stability JO: Virology http://www.kidney.de/pget.php?&tw=1&pmid=34217923 #FOAvip The fall of 2020 brought several new variants of SARS-CoV-2 circulating across the globe, and the steadily increasing COVID-19 cases are responsible for the emergence of these variants. All the SARS-CoV-2 variants reported to date have multiple mutations in the spike (S) protein, specifically in the receptor-binding domain (RBD). Here, we employed an integrated computational approach involving structure and sequence based predictions to study the effect of naturally occurring variations in the S-RBD on its stability and ACE2 binding affinity. The hotspot stabilizing residue mutations N501I, N501Y, Q493L, Q493H and K417R, strengthen the RBD-ACE2 complex by modulating the interaction statistics at the interface. Thus, we report here some critical mutations that could increase the binding affinity of the SARS-CoV-2 RBD with ACE2, increasing the viral infectivity and pathogenicity. Understanding the effect of these mutations will help in developing potential vaccines and therapeutics. Twit Text FOAVip Insilico study on the effect of SARS-CoV-2 RBD hotspot mutants interaction with ACE2 to understand the binding affinity and stability ????Virology http://www.kidney.de/pget.php?&tw=1&pmid=34217923 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34217923 #FOAvip English Wikipedia <ref>{{Cite pmid|34217923}}</ref> Insilico study on the effect of SARS-CoV-2 RBD hotspot mutants interaction with ACE2 to understand the binding affinity and stability #MMPMID34217923 Verma J; Subbarao N Virology 2021[Sep]; 561 (ä): 107-116 PMID34217923show ga The fall of 2020 brought several new variants of SARS-CoV-2 circulating across the globe, and the steadily increasing COVID-19 cases are responsible for the emergence of these variants. All the SARS-CoV-2 variants reported to date have multiple mutations in the spike (S) protein, specifically in the receptor-binding domain (RBD). Here, we employed an integrated computational approach involving structure and sequence based predictions to study the effect of naturally occurring variations in the S-RBD on its stability and ACE2 binding affinity. The hotspot stabilizing residue mutations N501I, N501Y, Q493L, Q493H and K417R, strengthen the RBD-ACE2 complex by modulating the interaction statistics at the interface. Thus, we report here some critical mutations that could increase the binding affinity of the SARS-CoV-2 RBD with ACE2, increasing the viral infectivity and pathogenicity. Understanding the effect of these mutations will help in developing potential vaccines and therapeutics. |*Binding Sites[MESH] |*Mutation[MESH] |*Protein Interaction Domains and Motifs[MESH] |Amino Acids[MESH] |Angiotensin-Converting Enzyme 2/*chemistry/metabolism[MESH] |COVID-19/metabolism/virology[MESH] |Humans[MESH] |Hydrogen Bonding[MESH] |Molecular Docking Simulation[MESH] |Molecular Dynamics Simulation[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |SARS-CoV-2/*genetics[MESH] |Spike Glycoprotein, Coronavirus/*chemistry/*genetics[MESH]Insilico study on the effect of SARS-CoV-2 RBD hotspot mutants intera(epmc).pdf DeepDyve Pubget Overpricing