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10.1080/07391102.2021.1927844 http://scihub22266oqcxt.onion/10.1080/07391102.2021.1927844 34029506!ä!34029506 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 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 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biomol+Struct+Dyn 2022 ; 40 (19): 9287-9305 Nephropedia Template TP {{tp|p=34029506|t=2022. Binding mode characterization of 13b in the monomeric and dimeric states of SARS-CoV-2 main protease using molecular dynamics simulations |pdf=|usr=}}{{34029506}} gab.com Text Binding mode characterization of 13b in the monomeric and dimeric states of SARS-CoV-2 main protease using molecular dynamics simulations JO: J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=34029506 #FOAvip The main protease, M(pro)/3CL(pro), plays an essential role in processing polyproteins translated from viral RNA to produce functional viral proteins and therefore serve as an attractive target for discovering COVID-19 therapeutics. The availability of both monomer and dimer crystal bound with a common ligand, '13b' (alpha-ketoamide inhibitor), opened up opportunities to understand the M(pro) mechanism of action. A comparative analysis of both forms of M(pro) was carried out to elucidate the binding site architectural differences in the presence and absence of '13b'. Molecular dynamics simulations suggest that the presence of '13b' enhances the stability of M(pro) than the unbound APO form. The N- and C- terminals of both the protomers stabilize each other, and making it's interface essential for the active form of M(pro). In comparison to monomer, the relatively high affinity of '13b' is gained in dimer pocket due to the high stability of the pocket by the interaction of S1 residue of chain B with residues F140, E166 and H172 of chain A, which is absent in monomer. The comprehensive essential dynamics, protein structure network analysis and thermodynamic profiling highlight the hot-spots, pivotal in molecular recognition process at protein-ligand and protein-protein interaction levels, cross-validated through computational alanine scanning study. A comparative description of '13b' binding mechanism in both forms illustrates valuable insights into the inhibition mechanism and the selection of critical residues suitable for the structure-based approaches for the identification of more potent M(pro) inhibitors.Communicated by Ramaswamy H. Sarma. Twit Text FOAVip Binding mode characterization of 13b in the monomeric and dimeric states of SARS-CoV-2 main protease using molecular dynamics simulations ????J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=34029506 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34029506 #FOAvip English Wikipedia <ref>{{Cite pmid|34029506}}</ref> Binding mode characterization of 13b in the monomeric and dimeric states of SARS-CoV-2 main protease using molecular dynamics simulations #MMPMID34029506 Kumari A; Mittal L; Srivastava M; Asthana S J Biomol Struct Dyn 2022[]; 40 (19): 9287-9305 PMID34029506show ga The main protease, M(pro)/3CL(pro), plays an essential role in processing polyproteins translated from viral RNA to produce functional viral proteins and therefore serve as an attractive target for discovering COVID-19 therapeutics. The availability of both monomer and dimer crystal bound with a common ligand, '13b' (alpha-ketoamide inhibitor), opened up opportunities to understand the M(pro) mechanism of action. A comparative analysis of both forms of M(pro) was carried out to elucidate the binding site architectural differences in the presence and absence of '13b'. Molecular dynamics simulations suggest that the presence of '13b' enhances the stability of M(pro) than the unbound APO form. The N- and C- terminals of both the protomers stabilize each other, and making it's interface essential for the active form of M(pro). In comparison to monomer, the relatively high affinity of '13b' is gained in dimer pocket due to the high stability of the pocket by the interaction of S1 residue of chain B with residues F140, E166 and H172 of chain A, which is absent in monomer. The comprehensive essential dynamics, protein structure network analysis and thermodynamic profiling highlight the hot-spots, pivotal in molecular recognition process at protein-ligand and protein-protein interaction levels, cross-validated through computational alanine scanning study. A comparative description of '13b' binding mechanism in both forms illustrates valuable insights into the inhibition mechanism and the selection of critical residues suitable for the structure-based approaches for the identification of more potent M(pro) inhibitors.Communicated by Ramaswamy H. Sarma. |*COVID-19[MESH] |*Molecular Dynamics Simulation[MESH] |Cysteine Endopeptidases/chemistry[MESH] |Humans[MESH] |Ligands[MESH] |Molecular Docking Simulation[MESH] |Protease Inhibitors/pharmacology/chemistry[MESH]Binding mode characterization of 13b in the monomeric and dimeric stat(epmc).pdf DeepDyve Pubget Overpricing