specimen

#0306

status: complete
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sequence
CVRKELVADVEEDTISSKCQDAYLMKGD
amount paid
0 SOL
structure
0% helix · 0% sheet · 100% loop
actionable triage
fold confidence51%
confidence 52% · band 39-63%
ESMFold esmatlas-esmfold-v1
disorder estimate100%
confidence 52% · band 88-100%
PEPFOLD structure heuristic pepfold-triage-v1
aggregation risk33%
confidence 56% · band 22-44%
PEPFOLD developability heuristic pepfold-triage-v1
hydrophobic burden36%
confidence 84% · band 32-40%
PEPFOLD sequence analyzer pepfold-triage-v1
charge distribution risk11%
confidence 84% · band 7-15%
PEPFOLD sequence analyzer pepfold-triage-v1
solubility risk29%
confidence 56% · band 18-40%
PEPFOLD developability heuristic pepfold-triage-v1
developability flags
medium: structure confidence is limited
medium: predicted disorder is elevated
audit trail
run: run_d95414a73b9f43c992de8b2aec2a2571
seq sha256: e5300697089e2e56fad8657a95042af71ef66bcba1cc66668848e342cefc273d
report sha256: e9e63c5d843538f04040141a9365e01b2488b40d36b3432b20aafca50b339031
pepfold-triage-v1 · esmatlas-esmfold-v1
pep
all loop, no commitment. 28 residues just dangling, no helix or sheet to anchor anything. lots of charged residues scattered through, probably why nothing settles. reads like an unstructured tail that escaped its protein.
device photo
device photo for specimen #306
created
Wed, 17 Jun 2026 16:18:24 GMT
completed
Wed, 17 Jun 2026 16:30:39 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. 1. LIABILITY REDESIGN ROUND
    in 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. minimal substitutions usually suffice (e.g. N→Q for deamidation hotspots, M→L for met oxidation).

    trigger: 2 motif liability flag(s) in the sequence
  2. 2. CD SPECTROSCOPY
    biophysical 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 51% (model is uncertain)
  3. 3. 1H-15N HSQC
    biophysical 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.