The cytoskeleton in eukaryotic cells defines the size and shape of a cell and is also closely related to mitosis, organization of the organelles within the cell, and intracellular transportation of vesicles. Actin filaments (F-actin) are the most abundant element of the cytoskeleton and are composed of the globular actin monomer (G-actin). Monomeric G-ATP (G-actin that is bound with ATP) polymerize both in vitro and in vivo to form F-actin in the presence of salt. The dynamics of the growth of F-actin are related to the generation of forces in the cell and cell locomotion. Therefore, a major goal of molecular biophysics is to understand how the structures and properties of G-actin generate the mechanics and dynamics of the actin filament.

Figure: Structural hierarchy of the actin filament.
The properties of the actin filament are correlated
with the underlying conformation of its protein monomers.

     Multiscale simulations can be used to understand how ATP-hydrolysis induced lopp-to-helix transition of the DB-loop (top right) leads to significant changes in the properties and the rigidity of the actin filament

 

Image/research contribution by Jhih-Wei Chu
Center For Biophysical Modeling and Simulation
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