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| Формат: | Recurso digital |
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| Опубліковано: |
Zenodo
2026
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| Предмети: | |
| Онлайн доступ: | https://doi.org/10.5281/zenodo.18229121 |
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Зміст:
- <p>The paper demonstrates that a single, fixed Ricker (Mexican-hat) wavelet, applied to mean-centered hydrophobicity sequences, produces statistically significant enrichment of long-range residue contacts in a subset of proteins whose folding is dominated by hydrophobic collapse. The method uses no per-protein tuning and is evaluated against a benchmark that includes both collapse-dominated proteins and mechanism-mismatched stress tests (e.g. disulfide-rich and membrane-associated structures).</p> <p> </p> <p>Key findings include:</p> <p> </p> <ul> <li>Emergence of a characteristic coherence scale in sequence space</li> <li>Order-of-magnitude enrichment of true long-range contacts in collapse-dominated proteins</li> <li>Clear mechanism specificity: the method succeeds selectively rather than universally</li> </ul> <p> </p> <p> </p> <p>The accompanying code package reproduces all figures and statistics reported in the manuscript, including:</p> <p> </p> <ul> <li>Kernel convolution and response rectification</li> <li>Contact enrichment and precision-lift metrics</li> <li>Benchmark and stress-test analyses </li> </ul>