Actomyosin Interaction: Mechanical and Energetic Properties in Different Nucleotide Binding States
AbstractThe mechanics of the actomyosin interaction is central in muscle contraction and intracellular trafficking. A better understanding of the events occurring in the actomyosin complex requires the examination of all nucleotide-dependent states and of the energetic features associated with the dynamics of the cross-bridge cycle. The aim of the present study is to estimate the interaction strength between myosin in nucleotide-free, ATP, ADP·Pi and ADP states and actin monomer. The molecular models of the complexes were constructed based on cryo-electron microscopy maps and the interaction properties were estimated by means of a molecular dynamics approach, which simulate the unbinding of the complex applying a virtual spring to the core of myosin protein. Our results suggest that during an ATP hydrolysis cycle the affinity of myosin for actin is modulated by the presence and nature of the nucleotide in the active site of the myosin motor domain. When performing unbinding simulations with a pulling rate of 0.001 nm/ps, the maximum pulling force applied to the myosin during the experiment is about 1nN. Under these conditions the interaction force between myosin and actin monomer decreases from 0.83 nN in the nucleotide-free state to 0.27 nN in the ATP state, and increases to 0.60 nN after ATP hydrolysis and Pi release from the complex (ADP state).
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Aprodu, I.; Redaelli, A.; Soncini, M. Actomyosin Interaction: Mechanical and Energetic Properties in Different Nucleotide Binding States. Int. J. Mol. Sci. 2008, 9, 1927-1943.
Aprodu I, Redaelli A, Soncini M. Actomyosin Interaction: Mechanical and Energetic Properties in Different Nucleotide Binding States. International Journal of Molecular Sciences. 2008; 9(10):1927-1943.Chicago/Turabian Style
Aprodu, Iuliana; Redaelli, Alberto; Soncini, Monica. 2008. "Actomyosin Interaction: Mechanical and Energetic Properties in Different Nucleotide Binding States." Int. J. Mol. Sci. 9, no. 10: 1927-1943.