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10.4314/ejhs.v31i2.2 http://scihub22266oqcxt.onion/10.4314/ejhs.v31i2.2 34158771!8188087!34158771     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Ethiop+J+Health+Sci 2021 ; 31 (2): 213-222 Nephropedia Template TP {{tp|p=34158771|t=2021. Functional and Structural Characterization of SARS-Cov-2 Spike Protein: An In Silico Study |pdf=|usr=}}{{34158771}} gab.com Text Functional and Structural Characterization of SARS-Cov-2 Spike Protein: An In Silico Study JO: Ethiop J Health Sci http://www.kidney.de/pget.php?&tw=1&pmid=34158771 #FOAvip BACKGROUND: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the cause of the global outbreak of coronavirus disease 2019 (Covid-19), which has been considered as a pandemic by WHO. SARS-CoV-2 encodes four major structural proteins, among which spike protein has always been a main target for new vaccine studies. This in silico study aimed to investigate some physicochemical, functional, immunological, and structural features of spike protein using several bioinformatics tools. METHOD: We retrieved all SARS-CoV-2 spike protein sequences from different countries registered in NCBI GenBank. CLC Sequence Viewer was employed to translate and align the sequences, and several programs were utilized to predict B-cell epitopes. Modification sites such as phosphorylation, glycosylation, and disulfide bonds were defined. Secondary and tertiary structures of all sequences were further computed. RESULTS: Some mutations were determined, where only one (D614G) had a high prevalence. The mutations did not impact the B-cell and physicochemical properties of the spike protein. Seven disulfide bonds were specified and also predicted in several N-link glycosylation and phosphorylation sites. The results also indicated that spike protein is a non-allergen. CONCLUSION: In summary, our findings provided a deep understanding of spike protein, which can be valuable for future studies on SARS-CoV-2 infections and design of new vaccines. Twit Text FOAVip Functional and Structural Characterization of SARS-Cov-2 Spike Protein: An In Silico Study ????Ethiop J Health Sci http://www.kidney.de/pget.php?&tw=1&pmid=34158771 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34158771 #FOAvip English Wikipedia <ref>{{Cite pmid|34158771}}</ref> Functional and Structural Characterization of SARS-Cov-2 Spike Protein: An In Silico Study #MMPMID34158771 Ebrahim-Saraie HS; Dehghani B; Mojtahedi A; Shenagari M; Hasannejad-Bibalan M Ethiop J Health Sci 2021[Mar]; 31 (2): 213-222 PMID34158771show ga BACKGROUND: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the cause of the global outbreak of coronavirus disease 2019 (Covid-19), which has been considered as a pandemic by WHO. SARS-CoV-2 encodes four major structural proteins, among which spike protein has always been a main target for new vaccine studies. This in silico study aimed to investigate some physicochemical, functional, immunological, and structural features of spike protein using several bioinformatics tools. METHOD: We retrieved all SARS-CoV-2 spike protein sequences from different countries registered in NCBI GenBank. CLC Sequence Viewer was employed to translate and align the sequences, and several programs were utilized to predict B-cell epitopes. Modification sites such as phosphorylation, glycosylation, and disulfide bonds were defined. Secondary and tertiary structures of all sequences were further computed. RESULTS: Some mutations were determined, where only one (D614G) had a high prevalence. The mutations did not impact the B-cell and physicochemical properties of the spike protein. Seven disulfide bonds were specified and also predicted in several N-link glycosylation and phosphorylation sites. The results also indicated that spike protein is a non-allergen. CONCLUSION: In summary, our findings provided a deep understanding of spike protein, which can be valuable for future studies on SARS-CoV-2 infections and design of new vaccines. |*COVID-19[MESH] |*Spike Glycoprotein, Coronavirus[MESH] |Computer Simulation[MESH] |Humans[MESH]Functional and Structural Characterization of SARS-Cov-2 Spike Protein(epmc).pdf DeepDyve Pubget Overpricing