Structural Validation and Membrane Interaction Analysis of ORF104 (Oblin-2) in Streptococcus sanguinis.
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2026
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| author | David Osvaldo, Carrillo Carranza |
| author_facet | David Osvaldo, Carrillo Carranza |
| contents | <p>This dataset provides the structural and topological validation of the micro-peptide <strong>ORF104 (Mexican Oblin-2)</strong>, identified in <em>Streptococcus sanguinis</em>. It features a high-resolution 3D model generated by <strong>AlphaFold 3 (Model 0)</strong>, revealing a well-defined amphipathic alpha-helix (residues 15-32) with a critical hydrophobic patch for membrane interaction.</p> <p>A comparative analysis between <strong>DeepTMHMM</strong> and <strong>HeliQuest</strong> is included, documenting a significant discrepancy between statistical predictors and molecular physics models. Notably, while DeepTMHMM suggests a globular cytoplasmic localization, this is likely a <strong>false negative due to the short length of the peptide (50 aa)</strong>, a known limitation for machine-learning-based topology predictors. Conversely, the structural evidence from AlphaFold 3 and the hydrophobic moment calculated via HeliQuest strongly support a membrane-anchored functional role.</p> |
| format | Recurso digital |
| id | zenodo_https___doi_org_10_5281_zenodo_19156514 |
| institution | Zenodo |
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| publishDate | 2026 |
| publisher | Zenodo |
| record_format | zenodo |
| spellingShingle | Structural Validation and Membrane Interaction Analysis of ORF104 (Oblin-2) in Streptococcus sanguinis. David Osvaldo, Carrillo Carranza Bioinformatics AlphaFold 3 Streptococcus sanguinis Membrane Proteins Structural Biology smORFs <p>This dataset provides the structural and topological validation of the micro-peptide <strong>ORF104 (Mexican Oblin-2)</strong>, identified in <em>Streptococcus sanguinis</em>. It features a high-resolution 3D model generated by <strong>AlphaFold 3 (Model 0)</strong>, revealing a well-defined amphipathic alpha-helix (residues 15-32) with a critical hydrophobic patch for membrane interaction.</p> <p>A comparative analysis between <strong>DeepTMHMM</strong> and <strong>HeliQuest</strong> is included, documenting a significant discrepancy between statistical predictors and molecular physics models. Notably, while DeepTMHMM suggests a globular cytoplasmic localization, this is likely a <strong>false negative due to the short length of the peptide (50 aa)</strong>, a known limitation for machine-learning-based topology predictors. Conversely, the structural evidence from AlphaFold 3 and the hydrophobic moment calculated via HeliQuest strongly support a membrane-anchored functional role.</p> |
| title | Structural Validation and Membrane Interaction Analysis of ORF104 (Oblin-2) in Streptococcus sanguinis. |
| topic | Bioinformatics AlphaFold 3 Streptococcus sanguinis Membrane Proteins Structural Biology smORFs |
| url | https://doi.org/10.5281/zenodo.19156514 |