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Protean

Candidate 20260613T025625Z-017

PPNQTSWPPNGQGTQWPG

Why this candidate advanced

Advanced for computational review because it showed compact fold and low exposed hydrophobic in the gpcr peptide campaign. This is a structural-prior signal only, not evidence of activity. The current computational decision is hold 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
hold for review
pLDDT
49.5
Compactness
0.768
Exposed hydrophobic
0.000
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_308f6cec4d4574f9 (18 aa) was advanced by Protean's structure-intelligence rerank as a hold for review within the GPCR peptide campaign.

Structural prior signals: compact fold, low exposed hydrophobic. pLDDT 49.5; compactness 0.768; exposed-hydrophobic 0.0.

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
PPNQTSWPPNGQGTQWPG
18 aa
gpcr_peptide
hydrophobic11%
polar44%
positive0%
negative0%
aromatic11%
C/P/G44%
deamidation motif
Fold evidence
very high 0%
confident 0%
low 56%
very low 44%
helix33%
sheet40%
coil27%
mean pLDDT
49.5
min pLDDT
45.0
compactness
0.768
exposed hydrophobic
0.000
radius of gyration
7.653
novelty
0.000
Computational decision
hold for review

Triage label: neutral

Evidence signatures

compact_fold, low_exposed_hydrophobic

low_confidence_disorder

ESMFold2 comparison
esmfold2-fast-2026-05 · folded
pLDDT 49.50 · 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
18 aa
Mol. weight
1.95 kDa
Net charge (pH 7.4)
-0.06
Isoelectric pt (pI)
6.10
GRAVY
-1.71
Aromaticity
11%
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.
P
P
N
Q
T
5
S
W
P
P
N
10
G
Q
G
T
Q
15
W
P
G

Provenance

provenance_hash: sha256:308f6cec4d4574f93e01934dd6ae1a1018a740d66df010713b57f5a17f7a8334
pdb_sha256: sha256:af0df0adfd63cafe739989ee766a2b1c1e46abb92f3aa8642129201d730f13f4
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