{
  "id": "cond-mat/0601533",
  "version": "v2",
  "published": "2006-01-24T09:55:17.000Z",
  "updated": "2006-01-28T09:47:49.000Z",
  "title": "Effective potentials for Folding Proteins",
  "authors": [
    "Nan-yow Chen",
    "Zheng-Yao Su",
    "Chung-Yu Mou"
  ],
  "comment": "4 pages, 4 figures, to appear in Physical Review Letters",
  "journal": "Phys. Rev. Lett. 96, 078103 (2006)",
  "doi": "10.1103/PhysRevLett.96.078103",
  "categories": [
    "cond-mat.stat-mech",
    "cond-mat.soft"
  ],
  "abstract": "A coarse-grained off-lattice model that is not biased in any way to the native state is proposed to fold proteins. To predict the native structure in a reasonable time, the model has included the essential effects of water in an effective potential. Two new ingredients, the dipole-dipole interaction and the local hydrophobic interaction, are introduced and are shown to be as crucial as the hydrogen bonding. The model allows successful folding of the wild-type sequence of protein G and may have provided important hints to the study of protein folding.",
  "revisions": [
    {
      "version": "v2",
      "updated": "2006-01-28T09:47:49.000Z"
    }
  ],
  "analyses": {
    "keywords": [
      "effective potential",
      "folding proteins",
      "local hydrophobic interaction",
      "dipole-dipole interaction",
      "fold proteins"
    ],
    "tags": [
      "journal article"
    ],
    "publication": {
      "publisher": "APS",
      "journal": "Phys. Rev. Lett."
    },
    "note": {
      "typesetting": "TeX",
      "pages": 4,
      "language": "en",
      "license": "arXiv",
      "status": "editable"
    }
  }
}