{
  "id": "cond-mat/9512111",
  "version": "v2",
  "published": "1995-12-14T01:42:32.000Z",
  "updated": "1997-01-05T01:03:27.000Z",
  "title": "Nature of Driving Force for Protein Folding -- A Result From Analyzing the Statistical Potential",
  "authors": [
    "Hao Li",
    "Chao Tang",
    "Ned Wingreen"
  ],
  "comment": "Revised version. 4 pages, Latex",
  "journal": "Phys. Rev. Lett. 79 (1997) 765",
  "doi": "10.1103/PhysRevLett.79.765",
  "categories": [
    "cond-mat.stat-mech",
    "physics.bio-ph",
    "q-bio.BM"
  ],
  "abstract": "In a statistical approach to protein structure analysis, Miyazawa and Jernigan (MJ) derived a $20\\times 20$ matrix of inter-residue contact energies between different types of amino acids. Using the method of eigenvalue decomposition, we find that the MJ matrix can be accurately reconstructed from its first two principal component vectors as $M_{ij}=C_0+C_1(q_i+q_j)+C_2 q_i q_j$, with constant $C$'s, and 20 $q$ values associated with the 20 amino acids. This regularity is due to hydrophobic interactions and a force of demixing, the latter obeying Hildebrand's solubility theory of simple liquids.",
  "revisions": [
    {
      "version": "v2",
      "updated": "1997-01-05T01:03:27.000Z"
    }
  ],
  "analyses": {
    "keywords": [
      "driving force",
      "statistical potential",
      "protein folding",
      "amino acids",
      "protein structure analysis"
    ],
    "tags": [
      "journal article"
    ],
    "publication": {
      "publisher": "APS",
      "journal": "Phys. Rev. Lett."
    },
    "note": {
      "typesetting": "LaTeX",
      "pages": 4,
      "language": "en",
      "license": "arXiv",
      "status": "editable"
    }
  }
}