{
  "annotation_id": "a5ef4121-0923-4704-aaa6-b47a68ee437f",
  "date_created": "2026-03-02T18:01:10.260000Z",
  "date_modified": "2026-03-02T18:01:10.260000Z",
  "file_hash": "f58020c68f33e4f32f3f30ff9bd361757a4f839498087e4aee0f082f86802799",
  "private": false,
  "record": {
    "abstract": "Evolutionally conserved quantity that specifies folding nuclei is pursued by\na case study for a small protein (PDB code: 1ten). First it is demonstrated\nthat the sequences of amino acids at folding nuclei are not conserved. Then 3D\n(3-dimensional) information of the structure is considered and it is found that\na 3D hydrophobicity profile is essential to specify the folding nuclei and\nevolutionally conserved. This profile is maintained by the interaction,\nincluding entropic effect, among amino acids realized in the native state\nstructure. Experimentally observed phi-value is correlated to this 3D\nhydrophobicity profile after taking into account the effect of the contact\ndistance in amino-acid sequence.",
    "arxiv_id": "physics/0607219",
    "authors": [
      "S. Nakamura",
      "O. Narikiyo"
    ],
    "categories": [
      "physics.bio-ph"
    ],
    "title": "A Mean-Field Description of Protein Folding: Evolutional Conservation of   Hydrophobicity Profile and Folding Nuclei",
    "url": "https://arxiv.org/abs/physics/0607219"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "8a6477fe-a385-4ea1-8582-3049881e3a2f",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}