DIRECT MEASUREMENT FOR ELASTICITY OF MYOSIN HEAD

被引：24

作者：

SUDA, H ^{[1
]}

SUGIMOTO, M ^{[1
]}

CHIBA, M ^{[1
]}

UEMURA, C ^{[1
]}

机构：

[1] TOKAI UNIV,DEPT MAT & TECHNOL,SHIZUOKA 41003,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 211卷 / 01期

关键词：

D O I：

10.1006/bbrc.1995.1799

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

During muscle contraction, chemical energy from ATP hydrolysis is converted to the relative sliding movement of actin and myosin filaments. Tn order to elucidate the molecular mechanism of sliding-force generation, it is a crucial clue to know an elastic modulus of myosin. Here, we report direct measurements of Young's modulus of myosin head (myosin subfragment-1) isolated from rabbit skeletal muscle, using a surface forces apparatus. Our results show that the elasticity of myosin subfragment-1 has direction and is about 0.3 GPa along the long axis during ATP hydrolysis. When the bow-shaped subfragment-1 is modelled as an elastic rod, the stiffness and the bending fluctuations of subfragment-1 are calculated to be 3 similar to 7 pN/nm and about 1 nm, respectively. These results strongly support a model of multiple power strokes rather than the conventional tilting-crossbridge model. (C) 1995 Academic Press, Inc.

引用

页码：219 / 225

页数：7

共 32 条

[1] ELLIPSOMETRY AS A TOOL TO STUDY ADSORPTION BEHAVIOR OF SYNTHETIC AND BIOPOLYMERS AT AIR-WATER-INTERFACE [J].