Decoding the Function of Protein 1i36 Through Sequence and Structural Analysis
Location
CoLab, COM 430
Start Date
30-4-2026 6:45 PM
Document Type
Poster
Description
Over 9000 protein structures determined through “High-Throughput Structure Determination” have unknown functions, creating a boundary between application and knowledge for future initiatives. Through bioinformatic tools, this project will aim to address those concerns to predict the functions of selected proteins. The protein 1i36 was analyzed using scientific websites: Protein Database, BLAST, InterPro, FoldSeek, and CLEAN were utilized to evaluate sequence similarity, structural features, and the possible enzymatic activity. The 1i36 protein was determined to have functions as an NAD(P)-dependent oxidoreductase. Interpro identified an NAD(P)-binding domain; BLAST results showed many similar proteins with oxidoreductase activity. Although the CLEAN application predicted a different enzyme class, a majority of the other evidence supports the protein's role in redox reactions and promotes the protein as a strong candidate for further studies.
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Decoding the Function of Protein 1i36 Through Sequence and Structural Analysis
CoLab, COM 430
Over 9000 protein structures determined through “High-Throughput Structure Determination” have unknown functions, creating a boundary between application and knowledge for future initiatives. Through bioinformatic tools, this project will aim to address those concerns to predict the functions of selected proteins. The protein 1i36 was analyzed using scientific websites: Protein Database, BLAST, InterPro, FoldSeek, and CLEAN were utilized to evaluate sequence similarity, structural features, and the possible enzymatic activity. The 1i36 protein was determined to have functions as an NAD(P)-dependent oxidoreductase. Interpro identified an NAD(P)-binding domain; BLAST results showed many similar proteins with oxidoreductase activity. Although the CLEAN application predicted a different enzyme class, a majority of the other evidence supports the protein's role in redox reactions and promotes the protein as a strong candidate for further studies.
Comments
The faculty mentor for this project was Faith Jacobsen.