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  1. B200 工学部/工学研究科
  2. B200a 雑誌掲載論文
  3. 学術雑誌

Coupling of Lever Arm Swing and Biased Brownian Motion in Actomyosin

http://hdl.handle.net/2237/20626
http://hdl.handle.net/2237/20626
130ad81d-c630-4b24-8d14-e8229bdd02c1
名前 / ファイル ライセンス アクション
journal_pcbi_1003552.pdf journal_pcbi_1003552.pdf (1.4 MB)
Item type 学術雑誌論文 / Journal Article(1)
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

WEKO 53860

en Nie, Qing-Miao

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Togashi, Akio

× Togashi, Akio

WEKO 53861

en Togashi, Akio

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Sasaki, Takeshi N.

× Sasaki, Takeshi N.

WEKO 53862

en Sasaki, Takeshi N.

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Takano, Mitsunori

× Takano, Mitsunori

WEKO 53863

en Takano, Mitsunori

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Sasai, Masaki

× Sasai, Masaki

WEKO 53864

en Sasai, Masaki

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Terada, Tomoki P.

× Terada, Tomoki P.

WEKO 53865

en 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
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
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