Identification of Unknown Protein 1p1m and its Biological Function in Metabolism using Bioinformation Tools
Location
CoLab, COM 409
Start Date
30-4-2026 5:30 PM
Document Type
Poster
Description
Many proteins from a variety of organisms have their sequence and structures determined and deposited into a large protein database. However, the biological functions still need to be further investigated. The goal of this project is to use bioinformatics tools to analyze the selected protein 1p1m and determine its potential biological function. To explore this protein, several bioinformatics tools were used, including BLAST for sequence similarity, InterPro for functional domain identification, FoldSeek for 3D structure similarities, and CLEAN for potential enzymatic activities. The analyses from BLAST, InterPro, FoldSeek and CLEAN consistently indicated protein 1p1m most likely functions as adenosine deaminase, suggesting that the protein may be a catalytic enzyme involved in the deamination of adenosine and its potential role in nucleotide metabolism.
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Identification of Unknown Protein 1p1m and its Biological Function in Metabolism using Bioinformation Tools
CoLab, COM 409
Many proteins from a variety of organisms have their sequence and structures determined and deposited into a large protein database. However, the biological functions still need to be further investigated. The goal of this project is to use bioinformatics tools to analyze the selected protein 1p1m and determine its potential biological function. To explore this protein, several bioinformatics tools were used, including BLAST for sequence similarity, InterPro for functional domain identification, FoldSeek for 3D structure similarities, and CLEAN for potential enzymatic activities. The analyses from BLAST, InterPro, FoldSeek and CLEAN consistently indicated protein 1p1m most likely functions as adenosine deaminase, suggesting that the protein may be a catalytic enzyme involved in the deamination of adenosine and its potential role in nucleotide metabolism.
Comments
The faculty mentor for this project was Faith Jacobsen.