{
  "annotation_id": "508e170c-3f2b-4e72-9c84-975dc2142493",
  "date_created": "2026-03-02T18:01:35.041000Z",
  "date_modified": "2026-03-02T18:01:35.041000Z",
  "file_hash": "c8729f5aef97e64d874be53652cd7b3875e8109a68e21179af5e0ade6d81ba5e",
  "private": false,
  "record": {
    "abstract": "The near-native free energy landscape of protein G is investigated through\n0.4 microseconds-long atomistic molecular dynamics simulations in explicit\nsolvent. A theoretical and computational framework is used to assess the\ntime-dependence of salient thermodynamical features. While the quasi-harmonic\ncharacter of the free energy is found to degrade in a few ns, the slow modes\ndisplay a very mild dependence on the trajectory duration. This property\noriginates from a striking self-similarity of the free energy landscape\nembodied by the consistency of the principal directions of the local minima,\nwhere the system dwells for several ns, and of the virtual jumps connecting\nthem.",
    "arxiv_id": "q-bio/0612020",
    "authors": [
      "F. Pontiggia",
      "G. Colombo",
      "C. Micheletti",
      "H. Orland"
    ],
    "categories": [
      "q-bio.BM",
      "cond-mat.soft",
      "physics.bio-ph"
    ],
    "doi": "10.1103/PhysRevLett.98.048102",
    "title": "Anharmonicity and self-similarity of the free energy landscape of   protein G",
    "url": "https://arxiv.org/abs/q-bio/0612020"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "c4b386f6-e84c-4485-b87b-1ee0ef5ba73c",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}