Volume 89, Number 3, February 2010
|Number of page(s)||6|
|Section||Interdisciplinary Physics and Related Areas of Science and Technology|
|Published online||22 February 2010|
Coupling of actin hydrolysis and polymerization: Reduced description with two nucleotide states
Max Planck Institute of Colloids and Interfaces - Science Park Golm, 14424 Potsdam, Germany, EU
2 Key Laboratory of Frontiers in Theoretical Physics, ITP, CAS - Beijing 100090, China
3 Physics Department, TU Dortmund University - 44221 Dortmund, Germany, EU
Corresponding author: Jan.Kierfeld@tu-dortmund.de
Accepted: 19 January 2010
The polymerization of actin filaments is coupled to the hydrolysis of adenosine triphosphate (ATP), which involves both the cleavage of ATP and the release of inorganic phosphate. We describe hydrolysis by a reduced two-state model with a cooperative cleavage mechanism, where the cleavage rate depends on the state of the neighboring actin protomer in a filament. We obtain theoretical predictions of experimentally accessible steady-state quantities such as the size of the ATP-actin cap, the size distribution of ATP-actin islands, and the cleavage flux for cooperative cleavage mechanisms.
PACS: 87.16.Ka – Filaments, microtubules, their networks, and supramolecular assemblies / 87.16.A- – Theory, modeling, and simulations / 87.15.rp – Polymerization
© EPLA, 2010
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