Modeling the bacterial flagellum by an elastic network of rigid bodies.

Abstract:

:Bacteria such as Escherichia coli propel themselves by rotating a bundle of helical filaments, each driven by a rotary motor embedded in the cell membrane. Each filament is an assembly of thousands of copies of the protein flagellin which assumes two different states. We model the filament by an elastic network of rigid bodies that form bonds with one another according to a scheme suggested by Namba and Vondervistz (1997 Q. Rev. Biophys. 30 1-65) and add additional binding sites at the inner part of the rigid body. Our model reproduces the helical parameters of the 12 possible polymorphic configurations very well. We demonstrate that its energetical ground state corresponds to the normal helical form, usually observed in nature, only when inner and outer binding sites of the rigid body have a large axial displacement. This finding correlates directly to the elongated shape of the flagellin molecule. An Ising Hamiltonian in our model directly addresses the two states of the flagellin protein. It contains an external field that represents external parameters which allow us to alter the ground state of the filament.

journal_name

Phys Biol

journal_title

Physical biology

authors

Speier C,Vogel R,Stark H

doi

10.1088/1478-3975/8/4/046009

subject

Has Abstract

pub_date

2011-08-01 00:00:00

pages

046009

issue

4

eissn

1478-3967

issn

1478-3975

pii

S1478-3975(11)87319-X

journal_volume

8

pub_type

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