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10.1016/j.csbj.2021.07.026 http://scihub22266oqcxt.onion/10.1016/j.csbj.2021.07.026 34336146!8312055!34336146     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Comput+Struct+Biotechnol+J 2021 ; 19 (ä): 4184-4191 Nephropedia Template TP {{tp|p=34336146|t=2021. Binding affinity and mechanisms of SARS-CoV-2 variants |pdf=|usr=}}{{34336146}} gab.com Text Binding affinity and mechanisms of SARS-CoV-2 variants JO: Comput Struct Biotechnol J http://www.kidney.de/pget.php?&tw=1&pmid=34336146 #FOAvip During the rapid worldwide spread of SARS-CoV-2, the viral genome has been undergoing numerous mutations, especially in the spike (S) glycoprotein gene that encode a type-I fusion protein, which plays an important role in the infectivity and transmissibility of the virus into the host cell. In this work, we studied the effect of S glycoprotein residue mutations on the binding affinity and mechanisms of SARS-CoV-2 using molecular dynamics simulations and sequence analysis. We quantitatively determined the degrees of binding affinity caused by different S glycoprotein mutations, and the result indicated that the 501Y.V1 variant yielded the highest enhancements in binding affinity (increased by 36.8%), followed by the N439K variant (increased by 29.5%) and the 501Y.V2 variant (increased by 19.6%). We further studied the structures, chemical bonds, binding free energies (enthalpy and entropy), and residue contribution decompositions of these variants to provide physical explanations for the changes in SARS-CoV-2 binding affinity caused by these residue mutations. This research identified the binding affinity differences of the SARS-CoV-2 variants and provides a basis for further surveillance, diagnosis, and evaluation of mutated viruses. Twit Text FOAVip Binding affinity and mechanisms of SARS-CoV-2 variants ????Comput Struct Biotechnol J http://www.kidney.de/pget.php?&tw=1&pmid=34336146 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34336146 #FOAvip English Wikipedia <ref>{{Cite pmid|34336146}}</ref> Binding affinity and mechanisms of SARS-CoV-2 variants #MMPMID34336146 Han Y; Wang Z; Wei Z; Schapiro I; Li J Comput Struct Biotechnol J 2021[]; 19 (ä): 4184-4191 PMID34336146show ga During the rapid worldwide spread of SARS-CoV-2, the viral genome has been undergoing numerous mutations, especially in the spike (S) glycoprotein gene that encode a type-I fusion protein, which plays an important role in the infectivity and transmissibility of the virus into the host cell. In this work, we studied the effect of S glycoprotein residue mutations on the binding affinity and mechanisms of SARS-CoV-2 using molecular dynamics simulations and sequence analysis. We quantitatively determined the degrees of binding affinity caused by different S glycoprotein mutations, and the result indicated that the 501Y.V1 variant yielded the highest enhancements in binding affinity (increased by 36.8%), followed by the N439K variant (increased by 29.5%) and the 501Y.V2 variant (increased by 19.6%). We further studied the structures, chemical bonds, binding free energies (enthalpy and entropy), and residue contribution decompositions of these variants to provide physical explanations for the changes in SARS-CoV-2 binding affinity caused by these residue mutations. This research identified the binding affinity differences of the SARS-CoV-2 variants and provides a basis for further surveillance, diagnosis, and evaluation of mutated viruses. äBinding affinity and mechanisms of SARS-CoV-2 variants (epmc).pdf DeepDyve Pubget Overpricing