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A mesoscopic model for helical bacterial flagella.

Benjamin Friedrich1

  • 1Max-Planck-Institute for Mathematics in the Sciences, Inselstrasse 22, 04103, Leipzig, Germany. benjamin.friedrich@mis.mpg.de

Journal of Mathematical Biology
|June 23, 2006
PubMed
Summary

Bacterial flagella filaments coil into essential helical shapes due to two flagellin protein states. This study models their spatial distribution to explain this crucial symmetry-breaking coiling.

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Area of Science:

  • Microbiology
  • Biophysics
  • Structural Biology

Background:

  • Bacterial flagella are helical filaments crucial for motility, built from flagellin protein monomers.
  • The helical structure arises from the coexistence of two flagellin conformational states, causing local misfit.
  • This misfit leads to the filament's essential curvature and twist for function.

Purpose of the Study:

  • To develop a coarse-grained model of bacterial flagella filaments.
  • To derive an elastic energy functional from the filament's microscopic structure.
  • To determine the spatial distribution of flagellin states and their role in helical formation.

Main Methods:

  • Developed a coarse-grained model for flagellar filaments.
  • Formulated an elastic energy functional based on microscopic structure.
  • Minimized the energy functional to predict flagellin state distribution.

Main Results:

  • Identified the spatial distribution of the two flagellin conformational states within the filament.
  • Explained how this distribution dictates the coupling of curvature and twist.
  • Extended Calladine's classical theory by predicting, rather than assuming, flagellin state distribution.

Conclusions:

  • The spatial arrangement of flagellin states is key to bacterial flagella's helical structure.
  • The model provides a mechanistic understanding of symmetry-breaking in biological filaments.
  • This work offers new insights into the biophysics of protein polymerization and cellular structures.

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