Name
Abstract | ||
|---|---|---|
A recent study with single molecule measurements has reported that muscle myosin, a molecular motor, stochastically generates multiple steps along an actin filament associated with the hydrolysis of a single ATP molecule [Kitamura, K., Tokunaga, M., Esaki, S., Iwane, A.H., Yanagida, T., 2005. Mechanism of muscle contraction based on stochastic properties of single actomyosin motors observed in vitro. Biophysics 1, 1–19]. We have built a model reproducing such a stochastic movement of a myosin molecule incorporated with ATPase reaction cycles and demonstrated that the thermal fluctuation was a key for the function of myosin molecules [Esaki, S., Ishii, Y., Yanagida, T., 2003. Model describing the biased Brownian movement of myosin. Proc. Jpn. Acad. 79 (Ser B), 9–14]. The size of the displacement generated during the hydrolysis of single ATP molecules was limited within a half pitch of an actin filament when a single myosin molecules work separately. However, in muscle the size of the displacement has been reported to be greater than 60nm [Yanagida, T., Arata, T., Oosawa, F., 1985. Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle. Nature 316, 366–369; Higuchi et al., 1991]. The difference suggests cooperative action between myosin heads in muscle. |
Year | DOI | Venue |
|---|---|---|
2007 | 10.1016/j.biosystems.2006.03.013 | Biosystems |
Keywords | Field | DocType |
Single molecule,Acto-myosin,Brownian movement,Cooperative action | Muscle contraction,Anatomy,Microfilament,Molecular motor,Biology,Myosin,Biophysics,Myosin filament,Actin,Genetics,Meromyosin,Myosin head | Journal |
Volume | Issue | ISSN |
88 | 3 | 0303-2647 |
Citations | PageRank | References |
4 | 1.54 | 0 |
Authors | ||
4 | ||
Name | Order | Citations | PageRank |
|---|---|---|---|
| Seiji Esaki | 1 | 16 | 3.00 |
| Yoshiharu Ishii | 2 | 17 | 4.46 |
| Masatoshi Nishikawa | 3 | 4 | 1.54 |
| Toshio Yanagida | 4 | 102 | 30.93 |