{
  "annotation_id": "6e32f939-e7e1-4ea4-bdfa-cadbe58bedfc",
  "date_created": "2026-03-02T18:01:31.932000Z",
  "date_modified": "2026-03-02T18:01:31.932000Z",
  "file_hash": "1dee4f14697dbe4d7caa57f5a437828d7f06c9005ff6e2943503070662995b6e",
  "private": false,
  "record": {
    "abstract": "We describe the results obtained from an improved model for protein folding.\nWe find that a good agreement with the native structure of a 46 residue long,\nfive-letter protein segment is obtained by carefully tuning the parameters of\nthe self-avoiding energy. In particular we find an improved free-energy\nprofile. We also compare the efficiency of the multidimensional replica\nexchange method with the widely used parallel tempering.",
    "arxiv_id": "q-bio/0503034",
    "authors": [
      "Andrea Nobile",
      "Federico Rapuano"
    ],
    "categories": [
      "q-bio.BM"
    ],
    "doi": "10.1088/0953-8984/18/24/009",
    "title": "Study of a model for the folding of a small protein",
    "url": "https://arxiv.org/abs/q-bio/0503034"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "4e907a49-a898-4a00-af0d-a6768eb20794",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}