{
  "annotation_id": "369a4c25-4ff7-46b9-841b-9650ddc31553",
  "date_created": "2026-03-02T18:01:34.858000Z",
  "date_modified": "2026-03-02T18:01:34.858000Z",
  "file_hash": "80423d9dfc9647cbb0793390d1000dfb97626b545f25dc51b0ed1400a56e8106",
  "private": false,
  "record": {
    "abstract": "The thermodynamics of the small SH3 protein domain is studied by means of a\nsimplified model where each bead-like amino acid interacts with the others\nthrough a contact potential controlled by a 20x20 random matrix. Good folding\nsequences, characterized by a low native energy, display three main\nthermodynamical phases, namely a coil-like phase, an unfolded globule and a\nfolded phase (plus other two phases, namely frozen and random coil, populated\nonly at extremes temperatures). Interestingly, the unfolded globule has some\nregions already structured. Poorly designed sequences, on the other hand,\ndisplay a wide transition from the random coil to a frozen state. The\ncomparison with the analytic theory of heteropolymers is discussed.",
    "arxiv_id": "q-bio/0512029",
    "authors": [
      "A. Amatori",
      "J. Ferkinghoff-Borg",
      "G. Tiana",
      "R. A. Broglia"
    ],
    "categories": [
      "q-bio.BM"
    ],
    "doi": "10.1103/PhysRevE.73.061905",
    "title": "What thermodynamic features characterize good and bad folders? Results   from a simplified off-lattice protein model",
    "url": "https://arxiv.org/abs/q-bio/0512029"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "8752d76a-6ec8-4e10-b1d6-c018bbb72a03",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}