{
  "annotation_id": "e5a09e7d-5d69-416e-9bc4-372cd55c0c48",
  "date_created": "2026-03-02T18:01:31.601000Z",
  "date_modified": "2026-03-02T18:01:31.601000Z",
  "file_hash": "9631755100bc6b3e4774d88564fad42303a01a87e4b2011a75ae7d11bee6f55a",
  "private": false,
  "record": {
    "abstract": "We study the folding thermodynamics of a beta-hairpin and two three-stranded\nbeta-sheet peptides using a simplified sequence-based all-atom model, in which\nfolding is driven mainly by backbone hydrogen bonding and effective hydrophobic\nattraction. The native populations obtained for these three sequences are in\ngood agreement with experimental data. We also show that the apparent native\npopulation depends on which observable is studied; the hydrophobicity energy\nand the number of native hydrogen bonds give different results. The magnitude\nof this dependence matches well with the results obtained in two different\nexperiments on the beta-hairpin.",
    "arxiv_id": "q-bio/0312042",
    "authors": [
      "Anders Irb\u00e4ck",
      "Fredrik Sjunnesson"
    ],
    "categories": [
      "q-bio.BM",
      "cond-mat.soft"
    ],
    "journal_ref": "Proteins 56 (2004) 110-116",
    "title": "Folding thermodynamics of three beta-sheet peptides: A model study",
    "url": "https://arxiv.org/abs/q-bio/0312042"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "086ee964-9987-41e6-9320-203968672180",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}