Block-type intrinsically disordered protein
A novel 376-residue intrinsically disordered protein: 100% predicted disorder, no folded domain, and a block architecture of alternating poly-Ala and poly-Gly runs with GPG turns. A converged 410 ns CALVADOS 2 ensemble shows an expanded self-avoiding-walk coil (Rg 5.66 nm, ν 0.562) with no persistent intramolecular contacts. No detectable homology in nr, and no structural neighbour in PDB, AlphaFold DB or ESM metagenomic databases.
evo_c137 is a novel 376-residue intrinsically disordered protein (IDP) built from alternating poly-alanine and poly-glycine blocks with GPG turn motifs and no folded domain. Sequence analysis predicts 100% disorder. A converged CALVADOS 2 simulation shows an expanded, fast-exchanging random coil in solution: one free-energy basin, no discrete states and no persistent intramolecular contacts. Throughout this dossier, REF marks the single atomistic reference conformation that seeds the simulation, ENS marks results from the simulated ensemble, and SEQ marks results computed from the sequence alone.
Block-type IDPs sit between a soluble, processable polymer and an assembling material, and this candidate is characterized at both ends. The ensemble is a soluble, expanded coil with predictable dimensions (Rg 5.66 nm, Rh 4.15 nm) that a partner can check by SAXS or DLS in a day. Sequence-based predictors flag its poly-Ala and poly-Gly blocks as aggregation-prone, which makes them candidate elements for β-assembly on processing; this remains untested. It has no detectable homolog in nr, no structural neighbour in PDB, AlphaFold DB or ESM metagenomic databases, and no known bioactive motif, and each use case below comes with a decisive first experiment.
No close family partner in the Atlas yet — this candidate is currently a singleton (family F0003). 7 candidates fall below the same-fold threshold (TM 0.119–0.463); none reaches TM > 0.5.
Note: whole-chain TM-align is less meaningful for disordered chains (flagged in source report) — read this as sequence-and-shape-class kinship, not a folded-protein identity match.
Full composition, motif coordinates, and simulation trajectories are released to evaluating partners on request.
