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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Xie, Ping |
| Description | Author Affiliation: Xie P ( Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China. pxie@aphy.iphy.ac.cn) |
| Abstract | F $_{1}$ -ATPase catalyzes ATP hydrolysis to drive the central γ-shaft rotating inside a hexameric cylinder composed of alternating α and β subunits. Experiments showed that the rotation of γ-shaft proceeds in steps of 120° and each 120°-rotation is composed of an 80° substep and a 40° substep. Here, based on the previously proposed models, an improved physical model for chemomechanical coupling of F $_{1}$ -ATPase is presented, with which the two-substep rotation is well explained. One substep is driven by the power stroke upon ATP binding, while the other one resulted from the passage of γ-shaft from previous to next adjacent β subunits via free diffusion. Using the model, the dynamics and kinetics of F $_{1}$ -ATPase, such as the rotating time of each substep, the dwell time at each pause and the rotation rate, are analytically studied. The theoretical results obtained with only three adjustable parameters reproduce the available experimental data well. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 7 |
| Volume Number | 1787 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2009-07-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Molecular Motor Proteins Metabolism Proton-Translocating ATPases Catalysis Dimerization Kinetics Models, Chemical Protein Binding Protein Subunits Chemistry Rotation Time Factors Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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