{
  "annotation_id": "d3769971-dcb3-4da5-8955-5ab72d52d5b7",
  "date_created": "2026-03-02T18:01:31.660000Z",
  "date_modified": "2026-03-02T18:01:31.660000Z",
  "file_hash": "82e7d104a4e50bb3115e7b4547f5f1825ecebff58d1c2d7c30fa9614267922b9",
  "private": false,
  "record": {
    "abstract": "We have exactly enumerated all sequences and conformations of HP proteins\nwith chains of up to 19 monomers on the simple cubic lattice. For two variants\nof the hydrophobic-polar (HP) model, where only two types of monomers are\ndistinguished, we determined and statistically analyzed designing sequences,\ni.e., sequences that have a non-degenerate ground state. Furthermore we were\ninterested in characteristic thermodynamic properties of HP proteins with\ndesigning sequences. In order to be able to perform these exact studies, we\napplied an efficient enumeration method based on contact sets.",
    "arxiv_id": "q-bio/0405009",
    "authors": [
      "Reinhard Schiemann",
      "Michael Bachmann",
      "Wolfhard Janke"
    ],
    "categories": [
      "q-bio.BM",
      "cond-mat.stat-mech"
    ],
    "doi": "10.1063/1.1814941",
    "journal_ref": "J. Chem. Phys. 122, 114705(1-10) (2005).",
    "title": "Exact Sequence Analysis for Three-Dimensional HP Lattice Proteins",
    "url": "https://arxiv.org/abs/q-bio/0405009"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "06ebcf75-fe18-40a7-a733-57cc675bffd5",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}