{
  "annotation_id": "5f50dff4-6dee-43e3-9042-e6a3fe586b6f",
  "date_created": "2026-03-02T18:00:38.566000Z",
  "date_modified": "2026-03-02T18:00:38.566000Z",
  "file_hash": "79b9d568a2cb802dd5c08e77c4a048b90039c0f3f2c0d8675a4df2f0d21515ef",
  "private": false,
  "record": {
    "abstract": "Helix-coil transitions in poly-alanine molecules of length 10 are studied by\nmulticanonical Monte Carlo simulations. The solvation effects are included by\neither a distance-dependent dielectric permittivity or by a term that is\nproportional to the solvent-accessible surface area of the peptide. We found a\nstrong dependence of the characteristics of the helix-coil transition from the\ndetails of the solvation model.",
    "arxiv_id": "physics/0202034",
    "authors": [
      "Y. Peng",
      "U. H. E. Hansmann"
    ],
    "categories": [
      "physics.bio-ph",
      "q-bio"
    ],
    "doi": "10.1016/S0006-3495(02)75668-3",
    "journal_ref": "Biophysical Journal vol. 82 (2002) 3269-3276",
    "title": "Solvation model dependency of helix-coil transition in polyalanine",
    "url": "https://arxiv.org/abs/physics/0202034"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "30cb7876-14b3-4813-a691-aa12b703b694",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}