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10.1039/d1cc01449h http://scihub22266oqcxt.onion/10.1039/d1cc01449h 33942835!ä!33942835 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Chem+Commun+(Camb) 2021 ; 57 (43): 5314-5317 Nephropedia Template TP {{tp|p=33942835|t=2021. Influence of charge configuration on substrate binding to SARS-CoV-2 main protease |pdf=|usr=}}{{33942835}} gab.com Text Influence of charge configuration on substrate binding to SARS-CoV-2 main protease JO: Chem Commun (Camb) http://www.kidney.de/pget.php?&tw=1&pmid=33942835 #FOAvip While the state-of-the-art computational simulations support the neutral state for the catalytic dyad of the SARS-CoV-2 main protease, the recently-reported neutron structure exhibits a zwitterionic form. To better compare the structural and dynamical features of the two charge configurations, we perform a Molecular Dynamics study of the dimeric enzyme in complex with a peptide substrate. The simulations show that the enzyme charge configuration from the neutron structure is not compatible with a catalytically-competent binding mode for peptide substrates. Twit Text FOAVip Influence of charge configuration on substrate binding to SARS-CoV-2 main protease ????Chem Commun (Camb) http://www.kidney.de/pget.php?&tw=1&pmid=33942835 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33942835 #FOAvip English Wikipedia <ref>{{Cite pmid|33942835}}</ref> Influence of charge configuration on substrate binding to SARS-CoV-2 main protease #MMPMID33942835 Diaz N; Suarez D Chem Commun (Camb) 2021[May]; 57 (43): 5314-5317 PMID33942835show ga While the state-of-the-art computational simulations support the neutral state for the catalytic dyad of the SARS-CoV-2 main protease, the recently-reported neutron structure exhibits a zwitterionic form. To better compare the structural and dynamical features of the two charge configurations, we perform a Molecular Dynamics study of the dimeric enzyme in complex with a peptide substrate. The simulations show that the enzyme charge configuration from the neutron structure is not compatible with a catalytically-competent binding mode for peptide substrates. |Amino Acid Sequence[MESH] |Catalytic Domain[MESH] |Crystallography, X-Ray[MESH] |Molecular Dynamics Simulation[MESH] |Peptide Hydrolases/*chemistry[MESH] |Peptides[MESH] |Protein Conformation[MESH]Influence of charge configuration on substrate binding to SARS-CoV-2 m(epmc).pdf DeepDyve Pubget Overpricing