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Proteins and polymers.

Jayanth R Banavar1, Trinh Xuan Hoang, Amos Maritan

  • 1Department of Physics, 104 Davey Laboratory, The Pennsylvania State University, University Park, Pennsylvania 16802, USA. banavar@psu.edu

The Journal of Chemical Physics
|July 13, 2005
PubMed
Summary
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The Flory theorem applies to protein structures, reconciling polymer physics with protein folding. Chain thickness is key to understanding protein behavior and structure.

Area of Science:

  • Biophysics
  • Polymer Physics
  • Structural Biology

Background:

  • Proteins are chain molecules of amino acids with unique behaviors distinct from standard polymers.
  • Understanding protein structure-function relationships is crucial in molecular biology and medicine.

Purpose of the Study:

  • To investigate the applicability of the Flory theorem to protein native state structures.
  • To explore the role of polymer chain thickness in protein physics.

Main Methods:

  • Analysis of protein native state structures.
  • Theoretical discussion on polymer chain thickness and its implications.

Main Results:

  • The Flory theorem, originally for polymer melts, is demonstrated to hold for compact protein native states.

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  • The theorem is compatible with protein structural motifs like alpha helices and beta strands.
  • Chain thickness is identified as a critical parameter bridging conventional polymer physics and protein structure.

    • Conclusions:

    • Protein structures can be described using principles of polymer physics, specifically the Flory theorem.
    • The concept of chain thickness is essential for a unified understanding of polymer and protein matter.
    • This work provides a new perspective on the physical underpinnings of protein folding and stability.