SINGLE MYOSIN MOLECULE MECHANICS - PICONEWTON FORCES AND NANOMETER STEPS

被引：1525

作者：

FINER, JT

SIMMONS, RM

SPUDICH, JA

机构：

[1] STANFORD UNIV,SCH MED,BECKMAN CTR,DEPT BIOCHEM,STANFORD,CA 94305

[2] STANFORD UNIV,SCH MED,BECKMAN CTR,DEPT BIOL,STANFORD,CA 94305

[3] KINGS COLL LONDON,RANDALL INST,MRC MUSCLE & CELL MOTIL UNIT,LONDON WC2B 5RL,ENGLAND

来源：

NATURE | 1994年 / 368卷 / 6467期

基金：

英国惠康基金;

关键词：

D O I：

10.1038/368113a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：113 / 119

页数：7

共 45 条

[1]

BAGSHAW CR, 1993, MUSCLE CONTRACTION, P98

[2] ROTATIONAL-DYNAMICS OF ACTIN-BOUND MYOSIN HEADS IN ACTIVE MYOFIBRILS [J].