{
  "annotation_id": "9cf9d57d-5c7e-40b8-91f8-e4bd7272b7b4",
  "date_created": "2026-03-02T18:01:28.596000Z",
  "date_modified": "2026-03-02T18:01:28.596000Z",
  "file_hash": "33259751c1d2997a3a5bd88a113cd42e70c2c1c5202f0827d30752758f4ede09",
  "private": false,
  "record": {
    "abstract": "We analyze the dependence of thermal denaturation transition and folding\nrates of globular proteins on the number of amino acid residues, N. Using\nlattice Go models we show that DeltaT/T_F ~ N^-1, where T_F is the folding\ntransition temperature and DeltaT is the folding transition width. This finding\nis consistent with finite size effects expected for the systems undergoing a\nphase transition from a disordered to an ordered phase. The dependence of the\nfolding rates k_F on N for lattice models and the dataset of 57 proteins and\npeptides shows that k_F = k_F^0 exp(-CN^beta) provides a good fit, if 0 \u003c beta\n\u003c= 2/3 and C is a constant. We find that k_F = k_F^0 exp(-1.1N^0.5) with k_F^0\n=(0.4x10^-6 s)^-1 can estimate optimal protein folding rates to within an order\nof magnitude in most cases. By using this fit for a set of proteins with\nbeta-sheet topology we find that k_F^0 is approximately equal to k_U^0, the\nprefactor for unfolding rates. The maximum ratio of k_U^0/k_F^0 is 10 for this\nclass of proteins.",
    "arxiv_id": "q-bio/0310020",
    "authors": [
      "Mai Suan Li",
      "D. K. Klimov",
      "D. Thirumalai"
    ],
    "categories": [
      "q-bio.BM"
    ],
    "title": "Thermal denaturation and folding rates of single domain proteins: size   matters",
    "url": "https://arxiv.org/abs/q-bio/0310020"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "e555aa35-c16a-4b54-992f-d305c1fa05b6",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}