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10.1016/j.str.2021.04.006 http://scihub22266oqcxt.onion/10.1016/j.str.2021.04.006 33932324!8086150!33932324     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 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       Structure 2021 ; 29 (8): 834-845.e5 Nephropedia Template TP {{tp|p=33932324|t=2021. Conformational flexibility and structural variability of SARS-CoV2 S protein |pdf=|usr=}}{{33932324}} gab.com Text Conformational flexibility and structural variability of SARS-CoV2 S protein JO: Structure http://www.kidney.de/pget.php?&tw=1&pmid=33932324 #FOAvip Spike (S) glycoprotein of SARS-CoV2 exists chiefly in two conformations, open and closed. Most previous structural studies on S protein have been conducted at pH 8.0, but knowledge of the conformational propensities under both physiological and endosomal pH conditions is important to inform vaccine development. Our current study employed single-particle cryoelectron microscopy to visualize multiple states of open and closed conformations of S protein at physiological pH 7.4 and near-physiological pH 6.5 and pH 8.0. Propensities of open and closed conformations were found to differ with pH changes, whereby around 68% of S protein exists in open conformation at pH 7.4. Furthermore, we noticed a continuous movement in the N-terminal domain, receptor-binding domain (RBD), S2 domain, and stalk domain of S protein conformations at various pH values. Several key residues involving RBD-neutralizing epitopes are differentially exposed in each conformation. This study will assist in developing novel therapeutic measures against SARS-CoV2. Twit Text FOAVip Conformational flexibility and structural variability of SARS-CoV2 S protein ????Structure http://www.kidney.de/pget.php?&tw=1&pmid=33932324 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33932324 #FOAvip English Wikipedia <ref>{{Cite pmid|33932324}}</ref> Conformational flexibility and structural variability of SARS-CoV2 S protein #MMPMID33932324 Pramanick I; Sengupta N; Mishra S; Pandey S; Girish N; Das A; Dutta S Structure 2021[Aug]; 29 (8): 834-845.e5 PMID33932324show ga Spike (S) glycoprotein of SARS-CoV2 exists chiefly in two conformations, open and closed. Most previous structural studies on S protein have been conducted at pH 8.0, but knowledge of the conformational propensities under both physiological and endosomal pH conditions is important to inform vaccine development. Our current study employed single-particle cryoelectron microscopy to visualize multiple states of open and closed conformations of S protein at physiological pH 7.4 and near-physiological pH 6.5 and pH 8.0. Propensities of open and closed conformations were found to differ with pH changes, whereby around 68% of S protein exists in open conformation at pH 7.4. Furthermore, we noticed a continuous movement in the N-terminal domain, receptor-binding domain (RBD), S2 domain, and stalk domain of S protein conformations at various pH values. Several key residues involving RBD-neutralizing epitopes are differentially exposed in each conformation. This study will assist in developing novel therapeutic measures against SARS-CoV2. |Cryoelectron Microscopy[MESH] |Humans[MESH] |Hydrogen-Ion Concentration[MESH] |Models, Molecular[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |SARS-CoV-2/chemistry/*metabolism[MESH] |Single Molecule Imaging[MESH]Conformational flexibility and structural variability of SARS-CoV2 S p(epmc).pdf DeepDyve Pubget Overpricing