DisorderDuty
When AlphaFold draws part of a protein in pale, low-confidence colour, it is easy to read it as “wrong” or “unfinished”. Usually it means the opposite kind of thing: that stretch is intrinsically disordered — genuinely floppy — and that floppiness is often exactly how it works. Tag each low-pLDDT region Broken or Working, then see the live UniProt annotation prove what it does. Everything runs locally; nothing about you is collected.
This is the tool. Your call is scored against the region’s live UniProt functional annotations, fetched in your browser. The regions are listed in full below (works without JavaScript). A native version, when it ships, adds offline use; it never gates the web.
Loading the game… If it does not start, the full region guide below still works.
How to play. Press Start. A pale, low-pLDDT region is highlighted — decide Broken or Working (buttons or keys 1/B, 2/W). The live UniProt annotation is revealed and your call is scored. Press Enter or Next to continue.
Low confidence is not the same as wrong
AlphaFold’s pLDDT is a per-residue confidence. Very low pLDDT often flags a region that is intrinsically disordered — it has no single fixed shape because it does not need one. Those regions do real work: they wrap onto partners, carry chemical marks, and fold up only when they touch the right surface. Reading “pale” as “error” is misconception M05, and this game trains the opposite reflex: pale usually means flexible and working.
The regions
| Protein | Region | What it does |
|---|---|---|
| p53 TP53 · P04637 | N-terminal transactivation domain (TAD) (1–61) | Disordered, yet the business end — binds MDM2 and the transcription machinery. |
| p53 TP53 · P04637 | C-terminal regulatory domain (363–393) | Disordered and heavily modified; tunes DNA binding, a hub of post-translational marks. |
| Histone H3.1 H3C1 · P68431 | N-terminal tail (1–40) | The disordered canvas of the histone code — its modifications switch genes on and off. |
| Alpha-synuclein SNCA · P37840 | Membrane-binding region (1–95) | Intrinsically disordered; folds to a helix only on meeting a membrane — a shape that appears on contact. |
Methods & about
This is a teaching game, honest about being a simplification. Not every low-pLDDT region is a well-characterised functional element — but the curated regions here are documented intrinsically-disordered functional stretches, and the reveal fetches their live UniProt features (regions, binding sites, modified residues, motifs) as evidence. Structures are the real AlphaFold predictions; annotations are live from UniProt. The game keeps no score history, uses no accounts, and sends nothing anywhere.
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