ダウンロード数: 1988
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ファイル | 記述 | サイズ | フォーマット | |
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biophysics.7.113.pdf | 1.85 MB | Adobe PDF | 見る/開く |
タイトル: | Importance of water entropy in rotation mechanism of F1-ATPase |
著者: | Yoshidome, Takashi |
著者名の別形: | 吉留, 崇 |
キーワード: | Asymmetric packing water hydration entropy integral equation theory morphometric approach |
発行日: | 2011 |
出版者: | Biophysical Society of Japan |
誌名: | BIOPHYSICS |
巻: | 7 |
開始ページ: | 113 |
終了ページ: | 122 |
抄録: | We briefly review our theoretical study on the rotation scheme of F1-ATPase. In the scheme, the key factor is the water entropy which has been shown to drive a variety of self-assembly processes in biological systems. We decompose the crystal structure of F1-ATPase into three sub-complexes each of which is composed of the γ subunit, one of the β subunits, and two α subunits adjacent to them. The βE, βTP, and βDP subunits are involved in the sub-complexes I, II, and III, respectively. We calculate the hydration entropy of each sub-complex using a hybrid of the integral equation theory for molecular liquids and the morphometric approach. It is found that the absolute value of the hydration entropy follows the order, sub-complex I > sub-complex II > sub-complex III. Moreover, the differences are quite large, which manifests highly asymmetrical packing of F1-ATPase. In our picture, this asymmetrical packing plays crucially important roles in the rotation of the γ subunit. We discuss how the rotation is induced by the water-entropy effect coupled with such chemical processes as ATP binding, ATP hydrolysis, and release of the products. |
著作権等: | (c) 2011 THE BIOPHYSICAL SOCIETY OF JAPAN |
URI: | http://hdl.handle.net/2433/152166 |
DOI(出版社版): | 10.2142/biophysics.7.113 |
PubMed ID: | 27857599 |
出現コレクション: | 学術雑誌掲載論文等 |
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