e-Journal of Surface Science and Nanotechnology
Online ISSN : 1348-0391
ISSN-L : 1348-0391
Conference -Nano-org. & Func.-
Rotary-angle dependency of ATP-binding affinity of F1-ATPase
Shouichi SakakiharaHiroyuki Noji
Author information
JOURNAL FREE ACCESS

2004 Volume 2 Pages 241-243

Details
Abstract

F1-ATPase, which is a part of ATP synthase, catalyzes the hydrolysis of ATP by itself. F1-ATPase is a single-molecule motor driven by the energy liberated from ATP hydrolysis. This rotation have been confirmed by a single-molecule rotation assay. By use of magnetic beads as the probe of microscopic image, the rotation of F1-ATPase have been controlled by an electromagnetic system. It is expected that if the ATP-binding of F1 triggers the rotation, the affinity of ATP-binding changes with the rotation angle. This feature was studied experimentally using the electromagnetic system. [DOI: 10.1380/ejssnt.2004.241]

Content from these authors

この記事はクリエイティブ・コモンズ [表示 4.0 国際]ライセンスの下に提供されています。
https://creativecommons.org/licenses/by/4.0/deed.ja
Previous article
feedback
Top