{
  "annotation_id": "2aa98abc-87c4-4e12-9955-ad5f7e943f51",
  "date_created": "2026-03-02T18:01:35.011000Z",
  "date_modified": "2026-03-02T18:01:35.011000Z",
  "file_hash": "fd0bf8aaa6dbe16701c2190fef937155aafb0843fb3cab5dd5d9c78d52c6faa3",
  "private": false,
  "record": {
    "abstract": "We study a Michaelis-Menten reaction for a single two-state enzyme molecule,\nwhose transition rates between the two conformations are modulated by an\nharmonically oscillating external force. In particular, we obtain a range of\noptimal driving frequencies for changing the conformation of the enzyme thereby\ncontrolling the enzymatic activity (i.e. product formation). This analysis\ndemonstrates that it is, in principle, possible to obtain information about\nparticular rates within the kinetic scheme.",
    "arxiv_id": "q-bio/0611011",
    "authors": [
      "Michael A. Lomholt",
      "Michael Urbakh",
      "Ralf Metzler",
      "Joseph Klafter"
    ],
    "categories": [
      "q-bio.BM",
      "cond-mat.stat-mech"
    ],
    "doi": "10.1103/PhysRevLett.98.168302",
    "journal_ref": "Phys. Rev. Lett. 98, 168302 (2007)",
    "title": "Manipulating single enzymes by an external harmonic force",
    "url": "https://arxiv.org/abs/q-bio/0611011"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "a4a60bad-9d19-4668-9f0e-ec5edea77f47",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}