## Abstract

We briefly review our theoretical study on the rotation scheme of F_{1}-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 F_{1}-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 β_{E}, β_{TP}, and β_{DP} 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, subcomplex I > sub-complex II > sub-complex III. Moreover, the differences are quite large, which manifests highly asymmetrical packing of F_{1}-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.

Original language | English |
---|---|

Pages (from-to) | 113-122 |

Number of pages | 10 |

Journal | Biophysics |

Volume | 7 |

DOIs | |

Publication status | Published - 2011 |

Externally published | Yes |

## Keywords

- Asymmetric packing
- Hydration entropy
- Integral equation theory
- Morphometric approach
- Water

## ASJC Scopus subject areas

- Biophysics

## Fingerprint

Dive into the research topics of 'Importance of water entropy in rotation mechanism of F_{1}-ATPase'. Together they form a unique fingerprint.