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10.1021/acs.biochem.0c00462 http://scihub22266oqcxt.onion/10.1021/acs.biochem.0c00462 32931703!7518256!32931703     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 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       Biochemistry 2020 ; 59 (39): 3741-3756 Nephropedia Template TP {{tp|p=32931703|t=2020. Sequence Characterization and Molecular Modeling of Clinically Relevant Variants of the SARS-CoV-2 Main Protease |pdf=|usr=}}{{32931703}} gab.com Text Sequence Characterization and Molecular Modeling of Clinically Relevant Variants of the SARS-CoV-2 Main Protease JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=32931703 #FOAvip The SARS-CoV-2 main protease (M(pro)) is essential to viral replication and cleaves highly specific substrate sequences, making it an obvious target for inhibitor design. However, as for any virus, SARS-CoV-2 is subject to constant neutral drift and selection pressure, with new M(pro) mutations arising over time. Identification and structural characterization of M(pro) variants is thus critical for robust inhibitor design. Here we report sequence analysis, structure predictions, and molecular modeling for seventy-nine M(pro) variants, constituting all clinically observed mutations in this protein as of April 29, 2020. Residue substitution is widely distributed, with some tendency toward larger and more hydrophobic residues. Modeling and protein structure network analysis suggest differences in cohesion and active site flexibility, revealing patterns in viral evolution that have relevance for drug discovery. Twit Text FOAVip Sequence Characterization and Molecular Modeling of Clinically Relevant Variants of the SARS-CoV-2 Main Protease ????Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=32931703 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32931703 #FOAvip English Wikipedia <ref>{{Cite pmid|32931703}}</ref> Sequence Characterization and Molecular Modeling of Clinically Relevant Variants of the SARS-CoV-2 Main Protease #MMPMID32931703 Cross TJ; Takahashi GR; Diessner EM; Crosby MG; Farahmand V; Zhuang S; Butts CT; Martin RW Biochemistry 2020[Oct]; 59 (39): 3741-3756 PMID32931703show ga The SARS-CoV-2 main protease (M(pro)) is essential to viral replication and cleaves highly specific substrate sequences, making it an obvious target for inhibitor design. However, as for any virus, SARS-CoV-2 is subject to constant neutral drift and selection pressure, with new M(pro) mutations arising over time. Identification and structural characterization of M(pro) variants is thus critical for robust inhibitor design. Here we report sequence analysis, structure predictions, and molecular modeling for seventy-nine M(pro) variants, constituting all clinically observed mutations in this protein as of April 29, 2020. Residue substitution is widely distributed, with some tendency toward larger and more hydrophobic residues. Modeling and protein structure network analysis suggest differences in cohesion and active site flexibility, revealing patterns in viral evolution that have relevance for drug discovery. |*Models, Molecular[MESH] |*Mutation[MESH] |Betacoronavirus/*enzymology/*genetics[MESH] |Catalytic Domain[MESH] |Drug Discovery[MESH] |Evolution, Molecular[MESH] |Humans[MESH] |Molecular Structure[MESH] |Phylogeny[MESH] |Protease Inhibitors/chemistry[MESH] |SARS-CoV-2[MESH] |Sequence Analysis, Protein[MESH]Sequence Characterization and Molecular Modeling of Clinically Relevan(epmc).pdf DeepDyve Pubget Overpricing