Analyzing Protein 1P1M
Location
CoLab, COM 205
Start Date
30-4-2026 10:45 AM
Document Type
Poster
Description
In the early 2000s, the protein structure initiative generated thousands of protein structures with unknown structures, and now we have a protein database to identify commonality in proteins. The problem is that there are too many unknown functions to known proteins, but the solution is to use bioinformatic tools (AI) to predict their functions. To address the problem, I used BLAST for sequence homology, InterPro for domain and family analysis, FoldSeek for structural comparison, and CLEAN to predict potential enzymatic functions. The results from using the bioinformatic tools shows that 1p1m protein suggest that protein, 1P1M from Thermotoga maritima is likely a S-methyl-5′ thioadenosine deaminase based on similar structure and function to other known proteins concluding in common low sequences.
Image
Analyzing Protein 1P1M
CoLab, COM 205
In the early 2000s, the protein structure initiative generated thousands of protein structures with unknown structures, and now we have a protein database to identify commonality in proteins. The problem is that there are too many unknown functions to known proteins, but the solution is to use bioinformatic tools (AI) to predict their functions. To address the problem, I used BLAST for sequence homology, InterPro for domain and family analysis, FoldSeek for structural comparison, and CLEAN to predict potential enzymatic functions. The results from using the bioinformatic tools shows that 1p1m protein suggest that protein, 1P1M from Thermotoga maritima is likely a S-methyl-5′ thioadenosine deaminase based on similar structure and function to other known proteins concluding in common low sequences.
Comments
The faculty mentor for this project was Faith Jacobsen.