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10.1038/s41598-021-82849-2 http://scihub22266oqcxt.onion/10.1038/s41598-021-82849-2 33608565!7896093!33608565     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Rep 2021 ; 11 (1): 4257 Nephropedia Template TP {{tp|p=33608565|t=2021. Flexibility and mobility of SARS-CoV-2-related protein structures |pdf=|usr=}}{{33608565}} gab.com Text Flexibility and mobility of SARS-CoV-2-related protein structures JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=33608565 #FOAvip The worldwide CoVid-19 pandemic has led to an unprecedented push across the whole of the scientific community to develop a potent antiviral drug and vaccine as soon as possible. Existing academic, governmental and industrial institutions and companies have engaged in large-scale screening of existing drugs, in vitro, in vivo and in silico. Here, we are using in silico modelling of possible SARS-CoV-2 drug targets, as deposited on the Protein Databank (PDB), and ascertain their dynamics, flexibility and rigidity. For example, for the SARS-CoV-2 spike protein-using its complete homo-trimer configuration with 2905 residues-our method identifies a large-scale opening and closing of the S1 subunit through movement of the S[Formula: see text] domain. We compute the full structural information of this process, allowing for docking studies with possible drug structures. In a dedicated database, we present similarly detailed results for the further, nearly 300, thus far resolved SARS-CoV-2-related protein structures in the PDB. Twit Text FOAVip Flexibility and mobility of SARS-CoV-2-related protein structures ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=33608565 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33608565 #FOAvip English Wikipedia <ref>{{Cite pmid|33608565}}</ref> Flexibility and mobility of SARS-CoV-2-related protein structures #MMPMID33608565 Romer RA; Romer NS; Wallis AK Sci Rep 2021[Feb]; 11 (1): 4257 PMID33608565show ga The worldwide CoVid-19 pandemic has led to an unprecedented push across the whole of the scientific community to develop a potent antiviral drug and vaccine as soon as possible. Existing academic, governmental and industrial institutions and companies have engaged in large-scale screening of existing drugs, in vitro, in vivo and in silico. Here, we are using in silico modelling of possible SARS-CoV-2 drug targets, as deposited on the Protein Databank (PDB), and ascertain their dynamics, flexibility and rigidity. For example, for the SARS-CoV-2 spike protein-using its complete homo-trimer configuration with 2905 residues-our method identifies a large-scale opening and closing of the S1 subunit through movement of the S[Formula: see text] domain. We compute the full structural information of this process, allowing for docking studies with possible drug structures. In a dedicated database, we present similarly detailed results for the further, nearly 300, thus far resolved SARS-CoV-2-related protein structures in the PDB. |*COVID-19 Drug Treatment[MESH] |Antiviral Agents/*pharmacology/therapeutic use[MESH] |Binding Sites[MESH] |COVID-19/epidemiology/virology[MESH] |Crystallography, X-Ray[MESH] |Drug Development/*methods[MESH] |Humans[MESH] |Models, Molecular[MESH] |Pandemics/prevention & control[MESH] |Protein Binding[MESH] |Protein Domains/drug effects[MESH] |Protein Multimerization/drug effects[MESH] |Protein Subunits/drug effects/metabolism[MESH] |SARS-CoV-2/*drug effects/metabolism[MESH]Flexibility and mobility of SARS-CoV-2-related protein structures (epmc).pdf DeepDyve Pubget Overpricing