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Protean

Candidate 20260612T222653Z-027

FPDNMKFFEPCPPNQ

Why this candidate advanced

Advanced for computational review because it showed low exposed hydrophobic and ordered in the gpcr peptide campaign. This is a structural-prior signal only, not evidence of activity. The current computational decision is promote for review.

Next experimental question

Does this sequence show measurable gpcr peptide activity, target engagement, or useful stability under controlled assay conditions?

Structure

Loading structure…
Predicted structure (ESMFold). Computational prediction — not an experimental structure and not biological proof.

Structure Intelligence

Computational decision
promote for review
pLDDT
51.8
Compactness
0.614
Exposed hydrophobic
0.153
Disulfide feasible
no
Structural novelty
0.000
Fold family
fold_cluster_000
Route
esmfold2_sidecar
Predicted structure source
ESMFold2 sidecar

Computational structural priors only. ESMFold/ESMFold2 predictions are not experimental structures or evidence of activity.

Research narrative

This is a computational prioritization result, not evidence of biological activity. Candidate struct_e67200e0a3ae6202 (15 aa) was advanced by Protean's structure-intelligence rerank as a promote for review within the GPCR peptide campaign.

Structural prior signals: low exposed hydrophobic, ordered. pLDDT 51.8; compactness 0.6138; exposed-hydrophobic 0.1526.

Disulfide assessment: no feasible disulfide pattern detected.

Novelty: structural-novelty score 0.000; fold family fold_cluster_000 (family size 10). Nearest archived fold at structural distance 0.000.

Sequence brief

Residue composition
FPDNMKFFEPCPPNQ
15 aa
gpcr_peptide
hydrophobic27%
polar27%
positive7%
negative13%
aromatic20%
C/P/G33%
odd cysteine
Fold evidence
very high 0%
confident 0%
low 87%
very low 13%
helix50%
sheet25%
coil25%
mean pLDDT
51.8
min pLDDT
48.0
compactness
0.614
exposed hydrophobic
0.153
radius of gyration
9.000
novelty
0.000
Computational decision
promote for review

Triage label: favored

Evidence signatures

low_exposed_hydrophobic, ordered

ESMFold2 comparison
esmfold2-fast-2026-05 · folded
pLDDT 51.80 · pTM — · iPTM —

Sequence and structure signals are computational triage evidence. They do not establish activity, binding, stability, safety, or wet-lab readiness.

Sequence & model analysis

Physicochemical properties
Computed from sequence (ProtParam-style). Computational, not biological proof.
Length
15 aa
Mol. weight
1.81 kDa
Net charge (pH 7.4)
-1.13
Isoelectric pt (pI)
4.18
GRAVY
-1.00
Aromaticity
20%
Per-residue model confidence (pLDDT)
ESMFold per-residue confidence from the folded model (0–100).

No per-residue confidence available — a folded coordinate file has not been published for this candidate.

Hydropathy profile
Kyte–Doolittle windowed hydropathy. Positive = hydrophobic, negative = hydrophilic.
4.50-4.5hydrophilic ↓ / hydrophobic ↑ · window 5
Sequence (colored by hydrophobicity)
Each residue shaded by Kyte–Doolittle value; hover for position + score.
F
P
D
N
M
5
K
F
F
E
P
10
C
P
P
N
Q
15

Provenance

provenance_hash: sha256:e67200e0a3ae620233c3d805a39709d93c8cd1fe730e4a542f79c4aa48e75230
pdb_sha256: sha256:d21090844d17b6e5f24a59b11682f9dc9861cb75295162049c12521a22944a18
campaign: gpcr_peptide
ledger_record: not attested

computational structural prior; ESMFold/proxy prediction; not an experimental structure and not biological proof of fold, binding, stability, or activity