ArticleProceedings of the National Academy of Sciences of the United States of America2002
Conformational change of the actomyosin complex drives the multiple stepping movement.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Single molecule detection, thermal fluctuation and life.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017Review
- Thermal-induced force release in oxyhemoglobin.Scientific reports · 2015Article
- Coupling of lever arm swing and biased Brownian motion in actomyosin.PLoS computational biology · 2014Article
- Structural and kinetic mapping of side-chain exposure onto the protein energy landscape.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Unidirectional Brownian motion observed in an in silico single molecule experiment of an actomyosin motor.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Cooperativity, connectivity, and folding pathways of multidomain proteins.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Single molecule measurements and molecular motors.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2008Review
- Internal strain regulates the nucleotide binding site of the kinesin leading head.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Mechanism of muscle contraction based on stochastic properties of single actomyosin motors observedBiophysics (Nagoya-shi, Japan) · 2005Article
- Dynamical transition and proteinquake in photoactive yellow protein.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- The path to visualization of walking myosin V by high-speed atomic force microscopy.Biophysical reviewsArticle
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3 authors.
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Abstract
Actin-myosin (actomyosin) generates mechanical force by consuming ATP molecules. We apply the energy landscape perspective to address a controversial issue as to whether the myosin head moves with multiple steps after a single ATP hydrolysis or only a single mechanical event of the lever-arm swinging follows a single ATP hydrolysis. Here we propose a theoretical model in which the refolding of the partially unfolded actomyosin complex and the movement of the myosin head along the actin filament are coupled. A single ATP hydrolysis is followed by the formation of a high free-energy partially unfolded actomyosin complex, which then gradually refolds with a concomitant multiple stepping movement on the way to the lowest free-energy rigor state. The model quantitatively explains the single-molecular observation of the multiple stepping movement and is consistent with structural observations of the disorder in the actomyosin-binding process. The model also explains the observed variety in dwell time before each step, which is not accounted for by previous models, such as the lever-arm or ratchet models.
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