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10.1021/acscatal.0c03420 http://scihub22266oqcxt.onion/10.1021/acscatal.0c03420 C7556163!7556163!34192089     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       ACS+Catal 2020 ; 10 (ä): 12544-54 Nephropedia Template TP {{tp|p=34192089|t=2020. Unraveling the SARS-CoV-2 Main Protease Mechanism Using Multiscale Methods |pdf=|usr=}}{{34192089}} gab.com Text Unraveling the SARS-CoV-2 Main Protease Mechanism Using Multiscale Methods JO: ACS Catal http://www.kidney.de/pget.php?&tw=1&pmid=34192089 #FOAvip We present a detailed theoretical analysis of the reaction mechanism of proteolysis catalyzed by the main protease of SARS-CoV-2. Using multiscale simulation methods, we have characterized the interactions established by a peptidic substrate in the active site, and then we have explored the free energy landscape associated with the acylation and deacylation steps of the proteolysis reaction, characterizing the transition states of the process. Our mechanistic proposals can explain most of the experimental observations made on the highly similar ortholog protease of SARS-CoV. We point to some key interactions that may facilitate the acylation process and thus can be crucial in the design of more specific and efficient inhibitors of the main protease activity. In particular, from our results, the P1? residue can be a key factor to improve the thermodynamics and kinetics of the inhibition process. Twit Text FOAVip Unraveling the SARS-CoV-2 Main Protease Mechanism Using Multiscale Methods ????ACS Catal http://www.kidney.de/pget.php?&tw=1&pmid=34192089 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34192089 #FOAvip English Wikipedia <ref>{{Cite pmid|34192089}}</ref> Unraveling the SARS-CoV-2 Main Protease Mechanism Using Multiscale Methods #MMPMID34192089 Ramos-Guzmán CA; Ruiz-Pernía JJ; Tuńón I ACS Catal 2020[]; 10 (ä): 12544-54 PMID34192089show ga We present a detailed theoretical analysis of the reaction mechanism of proteolysis catalyzed by the main protease of SARS-CoV-2. Using multiscale simulation methods, we have characterized the interactions established by a peptidic substrate in the active site, and then we have explored the free energy landscape associated with the acylation and deacylation steps of the proteolysis reaction, characterizing the transition states of the process. Our mechanistic proposals can explain most of the experimental observations made on the highly similar ortholog protease of SARS-CoV. We point to some key interactions that may facilitate the acylation process and thus can be crucial in the design of more specific and efficient inhibitors of the main protease activity. In particular, from our results, the P1? residue can be a key factor to improve the thermodynamics and kinetics of the inhibition process. äUnraveling the SARS-CoV-2 Main Protease Mechanism Using Multiscale Met(epmc).pdf DeepDyve Pubget Overpricing