{
  "id": "1002.5024",
  "version": "v1",
  "published": "2010-02-26T16:37:17.000Z",
  "updated": "2010-02-26T16:37:17.000Z",
  "title": "Elastic energy of proteins and the stages of protein folding",
  "authors": [
    "Jinzhi Lei",
    "Kerson Huang"
  ],
  "journal": "Europhys Lett, 88 (2009), 68004",
  "doi": "10.1209/0295-5075/88/68004",
  "categories": [
    "cond-mat.stat-mech",
    "cond-mat.soft",
    "physics.bio-ph",
    "q-bio.BM"
  ],
  "abstract": "We propose a universal elastic energy for proteins, which depends only on the radius of gyration $R_{g}$ and the residue number $N$. It is constructed using physical arguments based on the hydrophobic effect and hydrogen bonding. Adjustable parameters are fitted to data from the computer simulation of the folding of a set of proteins using the CSAW (conditioned self-avoiding walk) model. The elastic energy gives rise to scaling relations of the form $R_{g}\\sim N^{\\nu}$ in different regions. It shows three folding stages characterized by the progression with exponents $\\nu = 3/5, 3/7, 2/5$, which we identify as the unfolded stage, pre-globule, and molten globule, respectively. The pre-globule goes over to the molten globule via a break in behavior akin to a first-order phase transition, which is initiated by a sudden acceleration of hydrogen bonding.",
  "revisions": [
    {
      "version": "v1",
      "updated": "2010-02-26T16:37:17.000Z"
    }
  ],
  "analyses": {
    "keywords": [
      "protein folding",
      "molten globule",
      "universal elastic energy",
      "first-order phase transition",
      "hydrogen bonding"
    ],
    "tags": [
      "journal article"
    ],
    "publication": {
      "journal": "EPL (Europhysics Letters)",
      "year": 2009,
      "month": "Dec",
      "volume": 88,
      "number": 6,
      "pages": 68004
    },
    "note": {
      "typesetting": "TeX",
      "pages": 0,
      "language": "en",
      "license": "arXiv",
      "status": "editable",
      "adsabs": "2009EL.....8868004L"
    }
  }
}