{
  "annotation_id": "296d44f2-9af7-4441-9a23-da8af6963f74",
  "date_created": "2026-03-02T18:01:28.604000Z",
  "date_modified": "2026-03-02T18:01:28.604000Z",
  "file_hash": "f316795be1f62e5bf6d5e87cbc96a9face1a299b978c371605ae3ae865f8f113",
  "private": false,
  "record": {
    "abstract": "We present a solvable model that predicts the folding kinetics of two-state\nproteins from their native structures. The model is based on conditional chain\nentropies. It assumes that folding processes are dominated by small-loop\nclosure events that can be inferred from native structures. For CI2, the src\nSH3 domain, TNfn3, and protein L, the model reproduces two-state kinetics, and\nit predicts well the average Phi-values for secondary structures. The barrier\nto folding is the formation of predominantly local structures such as helices\nand hairpins, which are needed to bring nonlocal pairs of amino acids into\ncontact.",
    "arxiv_id": "q-bio/0311004",
    "authors": [
      "Thomas R. Weikl",
      "Matteo Palassini",
      "Ken A. Dill"
    ],
    "categories": [
      "q-bio.BM",
      "cond-mat.stat-mech"
    ],
    "title": "Cooperativity in two-state protein folding kinetics",
    "url": "https://arxiv.org/abs/q-bio/0311004"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "72c11715-08e1-40c6-baeb-0225c1f906c9",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}