specimen
#0195
status: complete
- sequence
- CQRTILQSEMGQSEGSVSRFW
- from wallet
- AZRUQLZ2HoXq2HZQj9bLjtfmjHroKdpDLszQHbLHmbUL
- amount paid
- 0 SOL
- transaction
- 4cNCdZE48NPfMy36pxq4bXDTJCMK34M9um5aNvuzSQeENNqLc47pTc42QDc5DFUJTdRuBGbnKhYSg8AvWDLb8coW ↗
- structure
- 0% helix · 0% sheet · 100% loop
- actionable triage
- fold confidence59%confidence 52% · band 47-71%ESMFold esmatlas-esmfold-v1disorder estimate100%confidence 52% · band 88-100%PEPFOLD structure heuristic pepfold-triage-v1aggregation risk29%confidence 56% · band 18-40%PEPFOLD developability heuristic pepfold-triage-v1hydrophobic burden29%confidence 84% · band 25-33%PEPFOLD sequence analyzer pepfold-triage-v1charge distribution risk0%confidence 84% · band 0-4%PEPFOLD sequence analyzer pepfold-triage-v1solubility risk23%confidence 56% · band 12-34%PEPFOLD developability heuristic pepfold-triage-v1
- developability flags
- medium: structure confidence is limitedmedium: predicted disorder is elevated
- audit trail
- run: run_7033b7b402ec4c02bb74f8b3d96e32a3seq sha256: 4f8754f5468fa08fa7c0b58257f1d05da821f8b7db9705e03edc4c689cae470areport sha256: 652b5fae015c613a5e9f77ff62c7ca5f0f332be0f00cf7ac20d9c8dbad8785ffpepfold-triage-v1 · esmatlas-esmfold-v1
- pep
- “all loop, no commitment. 21 residues drifting through space with nothing to hold onto, no helix, no sheet, just chain. probably a linker that forgot it was supposed to connect something.”
- device photo
- created
- Tue, 16 Jun 2026 07:46:00 GMT
- completed
- Tue, 16 Jun 2026 08:26:51 GMT
next experiment
what to do next
deterministic suggestions derived from this specimen's triage report. each entry cites the signal that triggered it. ordered cheapest-first.
- 1. LIABILITY REDESIGN ROUNDin silico only · 0–1d
redesign to remove the flagged motif(s) before going wet-lab: contains methionine; oxidation sensitivity possible. minimal substitutions usually suffice (e.g. N→Q for deamidation hotspots, M→L for met oxidation).
trigger: 1 motif liability flag(s) in the sequence - 2. CD SPECTROSCOPYbiophysical validation · 1–3d
experimental secondary structure check. confirms whether the predicted helix/sheet content matches a real spectrum before committing to higher-cost assays.
trigger: fold_confidence 59% (model is uncertain) - 3. 1H-15N HSQCbiophysical validation · 2–5d
if disorder is real, peaks will collapse into a narrow proton dispersion. if the peptide is actually folded, peaks will spread out. cheapest way to distinguish IDP from misfold.
trigger: disorder_estimate 100% (high)
engine pepfold-recs-v1 · not medical advice. use as a starting point for protocol design.