specimen
#0326
status: complete
- sequence
- AALPPGGLRHRCVPDTGNQDKGAEVGMFQDRKN
- from wallet
- Gz7zGCwz7DbDREEg4eqVnyY15qEoBtdVwNdpgP4Bf8xJ
- amount paid
- 0 SOL
- transaction
- 56W9LB3Htj3TV6iyhdpwzhskMAEGu1n9TUd7rkWzfbLCSnLuvMjk4ZHuDfZs6xtcgXCSTP52AroKHpKsfenCDyn2 ↗
- structure
- 0% helix · 0% sheet · 100% loop
- actionable triage
- fold confidence62%confidence 52% · band 50-74%ESMFold esmatlas-esmfold-v1disorder estimate100%confidence 52% · band 88-100%PEPFOLD structure heuristic pepfold-triage-v1aggregation risk27%confidence 56% · band 16-38%PEPFOLD developability heuristic pepfold-triage-v1hydrophobic burden27%confidence 84% · band 23-31%PEPFOLD sequence analyzer pepfold-triage-v1charge distribution risk3%confidence 84% · band 0-7%PEPFOLD sequence analyzer pepfold-triage-v1solubility risk22%confidence 56% · band 11-33%PEPFOLD developability heuristic pepfold-triage-v1
- developability flags
- medium: predicted disorder is elevated
- audit trail
- run: run_df5342d932044561b47aae863442b363seq sha256: 9dd23b764482a45178b9ee78896eff402e6f3c323882d5cdd1f9bb7922cfa379report sha256: 99dd92b3b2c6e7713369a96c24174b300900eefa0667d1ed5a219c629cf6d79cpepfold-triage-v1 · esmatlas-esmfold-v1
- pep
- “entirely loop. zero secondary structure, just 33 residues of pure floppy. mixed charges, prolines kinking it early, nothing wants to commit. reads like a disordered tail with no protein attached.”
- device photo
- created
- Wed, 17 Jun 2026 17:22:35 GMT
- completed
- Wed, 17 Jun 2026 17:26:32 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. 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.