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Coupling of Lever Arm Swing and Biased Brownian Motion in Actomyosin
http://hdl.handle.net/2237/20626
http://hdl.handle.net/2237/20626130ad81d-c630-4b24-8d14-e8229bdd02c1
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
journal_pcbi_1003552.pdf (1.4 MB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||
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| 公開日 | 2014-10-30 | |||||
| タイトル | ||||||
| タイトル | Coupling of Lever Arm Swing and Biased Brownian Motion in Actomyosin | |||||
| 言語 | en | |||||
| 著者 |
Nie, Qing-Miao
× Nie, Qing-Miao× Togashi, Akio× Sasaki, Takeshi N.× Takano, Mitsunori× Sasai, Masaki× Terada, Tomoki P. |
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| アクセス権 | ||||||
| アクセス権 | open access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_abf2 | |||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | An important unresolved problem associated with actomyosin motors is the role of Brownian motion in the process of force generation. On the basis of structural observations of myosins and actins, the widely held lever-arm hypothesis has been proposed, in which proteins are assumed to show sequential structural changes among observed and hypothesized structures to exert mechanical force. An alternative hypothesis, the Brownian motion hypothesis, has been supported by single-molecule experiments and emphasizes more on the roles of fluctuating protein movement. In this study, we address the long-standing controversy between the lever-arm hypothesis and the Brownian motion hypothesis through in silico observations of an actomyosin system. We study a system composed of myosin II and actin filament by calculating free-energy landscapes of actin-myosin interactions using the molecular dynamics method and by simulating transitions among dynamically changing free-energy landscapes using the Monte Carlo method. The results obtained by this combined multi-scale calculation show that myosin with inorganic phosphate (Pi) and ADP weakly binds to actin and that after releasing Pi and ADP, myosin moves along the actin filament toward the strong-binding site by exhibiting the biased Brownian motion, a behavior consistent with the observed single-molecular behavior of myosin. Conformational flexibility of loops at the actin-interface of myosin and the N-terminus of actin subunit is necessary for the distinct bias in the Brownian motion. Both the 5.5–11 nm displacement due to the biased Brownian motion and the 3–5 nm displacement due to lever-arm swing contribute to the net displacement of myosin. The calculated results further suggest that the recovery stroke of the lever arm plays an important role in enhancing the displacement of myosin through multiple cycles of ATP hydrolysis, suggesting a unified movement mechanism for various members of the myosin family. | |||||
| 言語 | en | |||||
| 出版者 | ||||||
| 出版者 | PLOS | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプresource | http://purl.org/coar/resource_type/c_6501 | |||||
| タイプ | journal article | |||||
| 出版タイプ | ||||||
| 出版タイプ | VoR | |||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
| DOI | ||||||
| 関連タイプ | isVersionOf | |||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | https://doi.org/10.1371/journal.pcbi.1003552 | |||||
| ISSN | ||||||
| 収録物識別子タイプ | PISSN | |||||
| 収録物識別子 | 1553-734X | |||||
| 書誌情報 |
en : PLOS Computational Biology 巻 10, 号 4, p. e1003552-e1003552, 発行日 2014-04 |
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| 著者版フラグ | ||||||
| 値 | publisher | |||||
| URI | ||||||
| 識別子 | http://dx.doi.org/10.1371/journal.pcbi.1003552 | |||||
| 識別子タイプ | DOI | |||||
| URI | ||||||
| 識別子 | http://hdl.handle.net/2237/20626 | |||||
| 識別子タイプ | HDL | |||||
