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10.1002/elsc.202000106 http://scihub22266oqcxt.onion/10.1002/elsc.202000106 34140855!8182281!34140855     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=34140855&cmd=llinks): Failed to open stream: HTTP request failed! 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Purification and characterization of the receptor-binding domain of SARS-CoV-2 spike protein from Escherichia coli |pdf=|usr=}}{{34140855}} gab.com Text Purification and characterization of the receptor-binding domain of SARS-CoV-2 spike protein from Escherichia coli JO: Eng Life Sci http://www.kidney.de/pget.php?&tw=1&pmid=34140855 #FOAvip SARS-CoV-2 is responsible for a disruptive worldwide viral pandemic, and renders a severe respiratory disease known as COVID-19. Spike protein of SARS-CoV-2 mediates viral entry into host cells by binding ACE2 through the receptor-binding domain (RBD). RBD is an important target for development of virus inhibitors, neutralizing antibodies, and vaccines. RBD expressed in mammalian cells suffers from low expression yield and high cost. E. coli is a popular host for protein expression, which has the advantage of easy scalability with low cost. However, RBD expressed by E. coli (RBD-1) lacks the glycosylation, and its antigenic epitopes may not be sufficiently exposed. In the present study, RBD-1 was expressed by E. coli and purified by a Ni Sepharose Fast Flow column. RBD-1 was structurally characterized and compared with RBD expressed by the HEK293 cells (RBD-2). The secondary structure and tertiary structure of RBD-1 were largely maintained without glycosylation. In particular, the major beta-sheet content of RBD-1 was almost unaltered. RBD-1 could strongly bind ACE2 with a dissociation constant (K(D)) of 2.98 x 10(-8) M. Thus, RBD-1 was expected to apply in the vaccine development, screening drugs and virus test kit. Twit Text FOAVip Purification and characterization of the receptor-binding domain of SARS-CoV-2 spike protein from Escherichia coli ????Eng Life Sci http://www.kidney.de/pget.php?&tw=1&pmid=34140855 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34140855 #FOAvip English Wikipedia <ref>{{Cite pmid|34140855}}</ref> Purification and characterization of the receptor-binding domain of SARS-CoV-2 spike protein from Escherichia coli #MMPMID34140855 He Y; Qi J; Xiao L; Shen L; Yu W; Hu T Eng Life Sci 2021[Jun]; 21 (6): 453-460 PMID34140855show ga SARS-CoV-2 is responsible for a disruptive worldwide viral pandemic, and renders a severe respiratory disease known as COVID-19. Spike protein of SARS-CoV-2 mediates viral entry into host cells by binding ACE2 through the receptor-binding domain (RBD). RBD is an important target for development of virus inhibitors, neutralizing antibodies, and vaccines. RBD expressed in mammalian cells suffers from low expression yield and high cost. E. coli is a popular host for protein expression, which has the advantage of easy scalability with low cost. However, RBD expressed by E. coli (RBD-1) lacks the glycosylation, and its antigenic epitopes may not be sufficiently exposed. In the present study, RBD-1 was expressed by E. coli and purified by a Ni Sepharose Fast Flow column. RBD-1 was structurally characterized and compared with RBD expressed by the HEK293 cells (RBD-2). The secondary structure and tertiary structure of RBD-1 were largely maintained without glycosylation. In particular, the major beta-sheet content of RBD-1 was almost unaltered. RBD-1 could strongly bind ACE2 with a dissociation constant (K(D)) of 2.98 x 10(-8) M. Thus, RBD-1 was expected to apply in the vaccine development, screening drugs and virus test kit. �Purification and characterization of the receptor-binding domain of SA(epmc).pdf DeepDyve Pubget Overpricing