Journal
PHYSICAL REVIEW LETTERS
Volume 101, Issue 12, Pages -Publisher
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.101.128103
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Funding
- Special Coordination Funds for Promoting Science and Technology: Yuragi Project
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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.
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