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In this study, in silico analysis was performed to examine the various aspects of the ROP29 protein, such as physicochemical properties, potential T\u2010 and B\u2010cell epitopes, and other significant features. The research revealed that there were 55 possible sites for posttranslational modification in the ROP29 protein. The secondary structure of the ROP29 protein consists of a random coil, an alpha\u2010helix, and an extended strand, which account for 49.69%, 36.81%, and 13.50%, respectively. Moreover, a number of putative T\u2010 and B\u2010cell epitopes for ROP29 were found. The Ramachandran plot showed that 88.91% (crude model) and 97.54% (refine model) of the amino acid residues were located in the favored regions. Also, the testing of this protein\u2019s antigenicity and allergenicity showed that it was nonallergenic and immunogenic. Our results suggested that employing in silico tools to apply structural and functional predictions to the ROP29 protein can lower the likelihood that laboratory investigations will fail. This research served as a crucial foundation for further research. More research is required in the future in suitable animal model employing ROP29 alone or in combination with other antigens.<\/jats:p>","DOI":"10.1155\/2024\/1918202","type":"journal-article","created":{"date-parts":[[2024,7,26]],"date-time":"2024-07-26T10:35:07Z","timestamp":1721990107000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["In Silico Analysis of the ROP29 Protein as a Vaccine Candidate Against <i>Toxoplasma 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