ELECTRON-MICROSCOPY OF THE ACTIN-MYOSIN HEAD COMPLEX IN THE PRESENCE OF ATP

被引：48

作者：

FRADO, LL ^{[1
]}

CRAIG, R ^{[1
]}

机构：

[1] UNIV MASSACHUSETTS,SCH MED,DEPT CELL BIOL,55 LAKE AVE N,WORCESTER,MA 01655

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1992年 / 223卷 / 02期

关键词：

ELECTRON MICROSCOPY; ACTOMYOSIN; CROSS-BRIDGE CYCLE; STRUCTURE; ATPASE;

D O I：

10.1016/0022-2836(92)90659-8

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：

The structure of the actin-myosin head complex during the ATPase cycle has been studied by electron microscopy of negatively stained acto-heavy-meromyosin. In the absence of ATP, heavy meromyosin molecules generally showed a regular, angled appearance, with both heads attached to the actin filament. In the presence of ATP, attached molecules showed a less ordered structure, often with only one head attached. We conclude that configurations other than the rigor structure occur during the actomyosin cross-bridge cycle. © 1992.

引用

页码：391 / 397

页数：7

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