Hatori Kuniyuki, Sakamaki Jun'ichi, Honda Hajime, Shimada Katsuhiko, Matsuno Koichiro
Department of BioEngineering, Nagaoka University of Technology, Nagaoka 940-2188, Japan.
Biophys Chem. 2004 Feb 15;107(3):283-8. doi: 10.1016/j.bpc.2003.09.011.
An ATP-activated actin filament sliding on myosin molecules exhibited mechanical distortions or fluctuations both longitudinally and transversally along the filament. Although actin filaments exhibited a uniform sliding movement longitudinally as the ATP concentration increased, the longitudinal fluctuations were found to vary their magnitude with the concentration. The magnitude of longitudinal fluctuations reached its maximum at approximately 100 microM of the ATP concentration. The local enhancement of the longitudinal fluctuations as responding to changes in the ATP concentration is associated with a critical phenomenon bridging the two different kinds of mechanical distortions, either contractile or protractile ones, occurring within a sliding actin filament.
在肌球蛋白分子上滑动的ATP激活的肌动蛋白丝在沿丝的纵向和横向都表现出机械变形或波动。尽管随着ATP浓度的增加,肌动蛋白丝在纵向表现出均匀的滑动运动,但发现纵向波动的幅度随浓度而变化。纵向波动的幅度在ATP浓度约为100 microM时达到最大值。纵向波动对ATP浓度变化的局部增强与一种临界现象有关,该现象连接了在滑动的肌动蛋白丝内发生的两种不同类型的机械变形,即收缩性或伸展性变形。