Simultaneous measurement of individual ATPase and mechanical reactions by a single myosin molecule at work

Akihiko Ishijima, Hiroaki Kojima, Hiroto Tanaka, Toshio Yanagida

研究成果: Article査読

抄録

Based on techniques for single molecule imaging and nanomanipulation by optical tweezers, we have developed a new technique that allows simultaneous measurement of individual ATPase and mechanical reactions from a single myosin molecule during force generation. We show how the ATPase reaction couples to the mechanical reaction directly at the single molecule level. The results show that the myosin head can produce force even after releasing the bound nucleotide, probably ADP, suggesting that the chemical energy driven by ATP hydrolysis can be hysteretically stored in the myosin molecule. This view does not support a widely accepted hypothesis in which the force generation is tightly coupled to ligand dissociation.

本文言語English
ページ(範囲)16-23
ページ数8
ジャーナルOptical Review
6
1
DOI
出版ステータスPublished - 1999 1月 1

ASJC Scopus subject areas

  • 原子分子物理学および光学

フィンガープリント

「Simultaneous measurement of individual ATPase and mechanical reactions by a single myosin molecule at work」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル