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Solitons in alpha-helical proteins.

L Brizhik1, A Eremko, B Piette

  • 1Bogolyubov Instiute for Theoretical Physics, 03143 Kyiv, Ukraine. brizhik@bitp.kiev.ua

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|November 5, 2004
PubMed
Summary

Davydov-Scott solitons in alpha-helical proteins are investigated. Helical symmetry leads to unstable solitons, while symmetry-breaking solitons are stable and exhibit complex dynamics, including interspine oscillations.

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Area of Science:

  • Biophysics
  • Theoretical Physics
  • Materials Science

Background:

  • Davydov's solitons are theoretical quasiparticles proposed to explain energy transport in biological systems like alpha-helical proteins.
  • The steric Davydov-Scott model incorporates molecular structure and interactions to study these solitons.

Purpose of the Study:

  • To investigate the role of helical symmetry in the dynamics of Davydov-Scott solitons within alpha-helical proteins.
  • To analyze the formation, stability, and propagation characteristics of these solitons.

Main Methods:

  • Analytical and numerical methods were employed to solve the nonlinear equations governing the soliton dynamics.
  • The study focused on examining stationary soliton solutions and their stability properties.

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Main Results:

  • Solitons preserving helical symmetry were found to be dynamically unstable and decay rapidly.
  • A stable, low-energy soliton emerges from spontaneous breaking of local translational and helical symmetries.
  • This robust soliton exhibits a hybrid nature, formed from hybridized quasiparticle states, with a complex, modulated multihump structure.

Conclusions:

  • The study identifies a robust, hybrid soliton as the energetically favorable state in alpha-helical proteins.
  • Interspine oscillations observed in moving solitons are attributed to helical symmetry and the soliton's hybrid structure.
  • The frequency of these oscillations is directly proportional to the soliton's velocity.