{
  "annotation_id": "ac691d0d-c5a0-4939-848b-fb570c24c371",
  "date_created": "2026-03-02T18:00:42.474000Z",
  "date_modified": "2026-03-02T18:00:42.474000Z",
  "file_hash": "b34ced088f822ffb33838be4ceb238f9ea32637dac8fef468812481655ba66cc",
  "private": false,
  "record": {
    "abstract": "Window profiles of amino acids in protein sequences are taken as a\ndescription of the amino acid environment. The relative entropy or\nKullback-Leibler distance derived from profiles is used as a measure of\ndissimilarity for comparison of amino acids and secondary structure\nconformations. Distance matrices of amino acid pairs at different conformations\nare obtained, which display a non-negligible dependence of amino acid\nsimilarity on conformations. Based on the conformation specific distances\nclustering analysis for amino acids is conducted.",
    "arxiv_id": "physics/0211033",
    "authors": [
      "Xin Liu",
      "Li-mei Zhang",
      "Shan Guan",
      "Wei-Mou Zheng"
    ],
    "categories": [
      "physics.bio-ph",
      "physics.data-an",
      "q-bio"
    ],
    "doi": "10.1103/PhysRevE.67.051927",
    "journal_ref": "PRE 67,051927 (2003)",
    "title": "Distances and classification of amino acids for different protein   secondary structures",
    "url": "https://arxiv.org/abs/physics/0211033"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "edb1eef2-c9ad-4d99-ac87-5f2bc9920740",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}