{
  "annotation_id": "92541a6f-106d-4a2a-85d7-f865601fa080",
  "date_created": "2026-03-02T18:01:31.801000Z",
  "date_modified": "2026-03-02T18:01:31.801000Z",
  "file_hash": "bda08b20c135eb68e1dfb03081d5153b7326f385095548065c8b03bc3b5a8b72",
  "private": false,
  "record": {
    "abstract": "Phi-values are experimental measures of how the kinetics of protein folding\nis changed by single-site mutations. Phi-values measure energetic quantities,\nbut are often interpreted in terms of the structures of the transition state\nensemble. Here we describe a simple analytical model of the folding kinetics in\nterms of the formation of protein substructures. The model shows that\nPhi-values have both structural and energetic components. In addition, it\nprovides a natural and general interpretation of \"nonclassical\" Phi-values\n(i.e., less than zero, or greater than one). The model reproduces the\nPhi-values for 20 single-residue mutations in the alpha-helix of the protein\nCI2, including several nonclassical Phi-values, in good agreement with\nexperiments.",
    "arxiv_id": "q-bio/0507025",
    "authors": [
      "Claudia Merlo",
      "Ken A. Dill",
      "Thomas R. Weikl"
    ],
    "categories": [
      "q-bio.BM",
      "cond-mat.soft"
    ],
    "doi": "10.1073/pnas.0504171102",
    "journal_ref": "PNAS 102, 10171 (2005)",
    "title": "Phi-values in protein folding kinetics have energetic and structural   components",
    "url": "https://arxiv.org/abs/q-bio/0507025"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "b8fa5d0c-19a0-42a3-8fd8-40c178dc4678",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}