#0475
- sequence
- QREKKSGCKCSGIAQNDEIAGSKAAWLAQTREGATQTQAGSQDLALVPRMQFQQIPGPNN
- from wallet
- 9euVsSWvDLPNPVsRqc7qLwdMzApQzC4A8NnpjYpzUCoS
- amount paid
- 0 SOL
- transaction
- WKY46Bkryuk6X7yyRAERUCT5UprbVy6YRcWsJHCvWX2ZLTMyWkuPVguTzG1ERaPvXKnREJR4c6BnsTNgqVBdfsZ ↗
- structure
- 0% helix · 0% sheet · 100% loop
- actionable triage
- fold confidence48%confidence 52% · band 36-60%ESMFold esmatlas-esmfold-v1disorder estimate100%confidence 52% · band 88-100%PEPFOLD structure heuristic pepfold-triage-v1aggregation risk28%confidence 56% · band 18-40%PEPFOLD developability heuristic pepfold-triage-v1hydrophobic burden30%confidence 84% · band 26-34%PEPFOLD sequence analyzer pepfold-triage-v1charge distribution risk3%confidence 84% · band 0-7%PEPFOLD sequence analyzer pepfold-triage-v1solubility risk24%confidence 56% · band 13-35%PEPFOLD developability heuristic pepfold-triage-v1
- developability flags
- medium: structure confidence is limitedmedium: predicted disorder is elevated
- synthesis hints
- - sequence length >45 aa may reduce synthesis yield
- audit trail
- run: run_bfa0e1d9c30a49bf8a93d75f0f10428bseq sha256: 70bebe881972b84320a1f01f5dd6e7fc0d7b88ad621336f2ebd543dad4928a2dreport sha256: b1746a248359eee941166671fb2b682cee650b8c3c06989e4a0d0925a0e15e9cpepfold-triage-v1 · esmatlas-esmfold-v1
- pep
- “60 residues of pure loop. no structure at all, just a long floppy string drifting through space. lots of glutamines and alanines, nothing committing to a shape. reads like an intrinsically disordered region that escaped its protein.”
- device photo

- created
- Wed, 24 Jun 2026 13:43:39 GMT
- completed
- Wed, 24 Jun 2026 14:11:46 GMT
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, multiple cysteines; disulfide heterogeneity risk, long hydrophobic run may increase aggregation risk. minimal substitutions usually suffice (e.g. N→Q for deamidation hotspots, M→L for met oxidation).
trigger: 3 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 48% (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)