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Phys Rev Lett. 2008 Sep 19;101(12):128103. Epub 2008 Sep 19.

Fluctuation analysis of mechanochemical coupling depending on the type of biomolecular motors.

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1
Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan. masnishi@hiroshima-u.ac.jp

Abstract

Mechanochemical coupling was studied for myosin II and V consistently. The fluctuation in myosin V motility was determined by correlating the stochasticity of the ATPase reaction with regular displacements per one ATP, consistent with a tight mechanochemical coupling. In contrast, myosin II, working in an ensemble, was explained by a loose coupling, generating variable step sizes which depend on [ATP] and realizing a much larger step (200 nm) per one ATP than myosin V through its cooperativity at zero load. These different mechanics are ideal for their physiological functions.

PMID:
18851416
DOI:
10.1103/PhysRevLett.101.128103
[Indexed for MEDLINE]
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