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Stretching globular polymers. I. Single chains.

A Craig1, E M Terentjev

  • 1Cavendish Laboratory, University of Cambridge Madingley Road, Cambridge, CB3 OHE, United Kingdom.

The Journal of Chemical Physics
|September 16, 2005
PubMed
Summary
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We analyzed polymer chains in poor solvents, focusing on their force-extension behavior. This study models protein unfolding and polymer networks, considering chain stiffness and internal structure.

Area of Science:

  • Polymer Physics
  • Biophysics

Background:

  • Polymers in poor solvents exhibit complex force-extension behavior.
  • Semiflexibility and internal globule structure influence polymer mechanics.

Purpose of the Study:

  • To review the force-extension behavior of polymers collapsed in poor solvents.
  • To model ordered and disordered globules, including semiflexibility effects.
  • To provide a foundation for understanding cross-linked polymer networks.

Main Methods:

  • Theoretical review of polymer force-extension behavior.
  • Modeling of ordered and disordered polymer globules.
  • Application to protein unfolding and polymer networks.

Main Results:

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  • Semiflexibility significantly impacts polymer collapse and extension.
  • Ordered globules serve as models for disordered globule unbinding and protein unfolding.
  • Single-chain behavior informs the mechanics of cross-linked polymer networks.

    • Conclusions:

    • Understanding polymer globule mechanics is crucial for diverse applications.
    • The models presented are applicable to protein unfolding and networked polymers.
    • This work bridges single-chain polymer physics with macroscopic network properties.