{
  "annotation_id": "3da44a88-a167-493a-8fe0-27018deff2f7",
  "date_created": "2026-03-02T18:00:32.500000Z",
  "date_modified": "2026-03-02T18:00:32.500000Z",
  "file_hash": "004a78ca6c25c5ee7c66e26847fa70b1ebf532fe62292d5d5a90c4a3ee77e3e2",
  "private": false,
  "record": {
    "abstract": "Microtubule dynamic instability arises from the hydrolysis of GTP bound to\nthe beta-monomer of the tubulin dimer. The conformational change induced by\nhydrolysis is unknown, but microtubules disassemble into protofilaments of\nGDP-bound tubulin that curve away from the microtubule axis. This paper\npresents the unfolding of a portion of the tubulin molecule into the\nmicrotubule interior as a plausible, unifying explanation for diverse\nstructural and kinetic features of microtubules. This is the first specific\nstructural hypothesis for the hydrolysis induced conformational change of\ntubulin that simultaneously explains weakening of lateral bonds, bending about\nlongitudinal bonds, changes in protofilament supertwist associated with GTP\nhydrolysis, structural features of GDP-tubulin double rings, faster disassembly\nat higher temperatures and slower disassembly in the presence of glycerol and\ndeuterium oxide. The hypothesis suggests further theoretical investigations and\ndirect experimental tests.",
    "arxiv_id": "physics/0101078",
    "authors": [
      "Deborah Kuchnir Fygenson"
    ],
    "categories": [
      "physics.bio-ph",
      "cond-mat.soft",
      "q-bio.BM"
    ],
    "title": "A Unifying Hypothesis for the Conformational Change of Tubulin",
    "url": "https://arxiv.org/abs/physics/0101078"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "1b3b38b4-494e-4b82-b177-dddac6c1a152",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}