{
  "annotation_id": "6ff09afd-80cc-4aa7-9cc9-dd3eef5b8bf8",
  "date_created": "2026-03-02T18:01:34.735000Z",
  "date_modified": "2026-03-02T18:01:34.735000Z",
  "file_hash": "02cd3dbca73374424a23e4baf551b2a26aa415676601c2857d9a1a83265ba159",
  "private": false,
  "record": {
    "abstract": "The influence of thiol blocking on the resolution of basic proteins by\ntwo-dimensional electrophoresis was investigated. Cysteine blocking greatly\nincreased resolution and decreased streaking, especially in the basic region of\nthe gels. Two strategies for cysteine blocking were found to be efficient:\nclassical alkylation with maleimide derivatives and mixed disulfide exchange\nwith an excess of a low molecular weight disulfide. The effect on resolution\nwas significant enough to allow correct resolution of basic proteins with\nin-gel rehydration on wide gradients (e.g. 3-10 and 4-12), but anodic\ncup-loading was still required for basic gradients (e.g. 6-12 or 8-12). These\nresults demonstrate that thiol-related problems are not solely responsible for\nstreaking of basic proteins on two-dimensional gels.",
    "arxiv_id": "q-bio/0611079",
    "authors": [
      "Sylvie Luche",
      "H\u00e9l\u00e8ne Diemer",
      "Chistophe Tastet",
      "Mireille Chevallet",
      "Alain Van Dorsselaer",
      "Emmanuelle Leize-Wagner",
      "Thierry Rabilloud"
    ],
    "categories": [
      "q-bio.GN"
    ],
    "doi": "10.1002/pmic.200300589",
    "journal_ref": "Proteomics 4 (03/2004) 551-61",
    "title": "About thiol derivatization and resolution of basic proteins in   two-dimensional electrophoresis",
    "url": "https://arxiv.org/abs/q-bio/0611079"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "2c2195d5-2607-4a25-85a0-ad933cea6ca0",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}