Biomimetic Chemistry | Macromolecular Chemistry | Cytoskeleton | Macromolecular Assemblies & Machines
Internal lever arm model for Myosin II
A Bibó*, G Károlyi, M Kovács
*Corresponding author: A Bibó
Budapest University of Technology and Economics, Budapest, Hungary
F1000Posters 2011, 2: 395 (poster) [ENGLISH]
Poster [3.20 MB]
Presented at
Biochemical Society/Wellcome Trust Focused Meeting 2011 - Cellular cytoskeletal motor proteins ,
30 Mar - 1 Apr 2011, P068
Myosin’s lever plays a crucial role in force generation. A large rotation of the lever occurs during the ATP hydrolysis cycle. This rotation leads to lever priming when myosin is detached from actin, and a reverse rotation occurs during the actin-bound powerstroke. Much effort has been made towards understanding the chemomechanical basis of the powerstroke. Kinetic approaches use a set of discrete states to describe the motion of myosin, while molecular dynamic simulations attempt to take into account all or nearly all atoms at high computational demand.
Here we propose an overdamped elastic model in which every myosin head is composed of a small number of rigid bodies connected with springs. The model includes an internal lever within the motor domain in addition to the previously investigated lever.
Our minimal mechanical model is capable of reproducing the continuous motion of myosin, and giving an estimate for the stiffness of subdomains. The simplicity of the model allows simulations embracing hundreds of heads acting in a sarcomere. Configurations of rigid bodies can be assigned to known structural states, and the displacement of the internal lever can be considered as a reaction coordinate allowing linkage to kinetic approaches.
No relevant conflicts of interest declared.
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