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Ideal-Chain Collapse in Biopolymers

Biological Physics 2009-09-25 v2 Chemical Physics Biomolecules

Abstract

A conceptual difficulty in the Hooke's-law description of ideal Gaussian polymer-chain elasticity is sometimes apparent in analyses of experimental data or in physical models designed to simulate the behavior of biopolymers. The problem, the tendency of a chain to collapse in the absence of external forces, is examined in the following examples: DNA-stretching experiments, gel electrophoresis, and protein folding. We demonstrate that the application of a statistical-mechanically derived repulsive force, acting between the chain ends, whose magnitude is proportional to the absolute temperature and inversely proportional to the scalar end separation removes this difficulty.

Keywords

Cite

@article{arxiv.physics/0011067,
  title  = {Ideal-Chain Collapse in Biopolymers},
  author = {Richard M. Neumann},
  journal= {arXiv preprint arXiv:physics/0011067},
  year   = {2009}
}

Comments

9 pages, 2 figures, improved format