SINGLE MYOSIN MOLECULE MECHANICS - PICONEWTON FORCES AND NANOMETER STEPS
SINGLE MYOSIN MOLECULE MECHANICS - PICONEWTON FORCES AND NANOMETER STEPS
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DOI：
10.1038/368113a0
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发表时间：
1994-03-10
期刊：
影响因子：
64.8
通讯作者：
SPUDICH, JA
中科院分区：
文献类型：
--
作者：
FINER, JT;SIMMONS, RM;SPUDICH, JA
一种使用反馈增强型激光阱系统的新型体外测定法能够直接测量由单个肌球蛋白分子与单个悬浮的肌动蛋白丝相互作用所产生的力和位移。在低负荷条件下观察到平均为4 - 6纳米的离散的逐步运动，在等长条件下测量到平均为3 - 4皮牛的单个力瞬变。单个力和位移的大小与肌肉收缩的传统摆动横桥模型的预测相符。
注：原文中“averaging ai nm”可能有误，根据上下文推测可能是“averaging 4 - 6 nm”之类的表述，如果有更准确信息可进一步完善翻译。
A new in vitro assay using a feedback enhanced laser trap system allows direct measurement of force and displacement that results from the interaction of a single myosin molecule with a single suspended actin filament. Discrete stepwise movements averaging ai nm were seen under conditions of low load, and single force transients averaging 3-4 pN were measured under isometric conditions. The magnitudes of the single forces and displacements are consistent with predictions of the conventional swinging-crossbridge model of muscle contraction.