Identificação de uma possível lectina de Mimosa tenuiflora (Willd.) Poir em bancos de sequências genômicas e modelagem computacional da sua estrutura tridimensional
Lectins are proteins of non-immune origin that specifically bind to carbohydrates. These proteins are often found in legumes, where they perform functions such as protection against pathogens and insects. Given this, in recent years researchers have been awakening interest in its possible biotechnol...
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| Formato: | bachelorThesis |
| Idioma: | pt_BR |
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Universidade Federal do Rio Grande do Norte
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| Endereço do item: | https://repositorio.ufrn.br/handle/123456789/56016 |
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| Resumo: | Lectins are proteins of non-immune origin that specifically bind to carbohydrates. These proteins are often found in legumes, where they perform functions such as protection against pathogens and insects. Given this, in recent years researchers have been awakening interest in its possible biotechnological applications for agriculture. Thus, in this study, bioinformatics tools were used to search for lectin isoforms in Mimosa tenuiflora (Willd.) Poir, a legume species popularly known as jurema-preta. Genome sequences of this species were searched in a biological database, where the fastq files with the reads were downloaded with the SRA-Toolkit and subjected to quality analysis with FastQC. Data quality was improved with Trimmomatic software and normalized with BBNorm. After obtaining quality data, the species' genome was assembled using the “de novo assembly” approach with the Velvet program, where it was subsequently aligned with the primary sequence of a lectin from the species Prosopis alba using the tBLASTn tool, in which one of the contigs showed 98% similarity, indicating the existence of a probable lectin. The consensus nucleotide sequence resulting from the alignment of all contigs was subjected to modeling, using two software with different modeling approaches, to verify which would predict the best structure. The model generated by artificial intelligence, through the AlphaFold program, was the one that presented better quality compared to the Swiss-model model, generated by homology. The quality assessment of the models was carried out using the Swiss-Model server, where clashscore values, unfavorable rotations, long connections, bad angles and the Ramachandran Chart were assessed. The model obtained in this work of the jurema-preta lectin can assist in future studies for a more in-depth assessment of the interaction of this protein with other molecules, thus contributing to the advancement of knowledge in this area. |
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