{
  "annotation_id": "44fdb00a-ff90-4185-b96b-05654507b03c",
  "date_created": "2026-03-02T18:01:31.674000Z",
  "date_modified": "2026-03-02T18:01:31.674000Z",
  "file_hash": "2553bae5e6f61c547c814a5c35914561d462c2eb3230c867d443f7e6f580fe1b",
  "private": false,
  "record": {
    "abstract": "We fit the Fourier transforms of solvent accessibility and hydrophobicity\nprofiles of a representative set of proteins to a joint multi-variable\nGaussian. This allows us to separate the intrinsic tendencies of sequence and\nstructure profiles from the interactions that correlate them; for example, the\n$\\alpha$-helix periodicity in sequence hydrophobicity is dictated by the\nsolvent accessibility of structures. The distinct intrinsic tendencies of\nsequence and structure profiles are most pronounced at long periods, where\nsequence hydrophobicity fluctuates more, while solvent accessibility\nfluctuations are less than average. Interestingly, correlations between the two\nprofiles can be interpreted as the Boltzmann weight of the solvation energy at\nroom temperature.",
    "arxiv_id": "q-bio/0406019",
    "authors": [
      "Mehdi Yahyanejad",
      "Christopher B. Burge",
      "Mehran Kardar"
    ],
    "categories": [
      "q-bio.BM"
    ],
    "title": "Untangling influences of hydrophobicity on protein sequences and   structures",
    "url": "https://arxiv.org/abs/q-bio/0406019"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "d2168fa7-2643-44a4-8937-d1df867b8683",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}