A single myosin head moves along an actin filament with regular steps of 5.3 nanometres
- 1 January 1999
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 397 (6715) , 129-134
- https://doi.org/10.1038/16403
Abstract
Actomyosin, a complex of actin filaments and myosin motor proteins, is responsible for force generation during muscle contraction. To resolve the individual mechanical events of force generation by actomyosin, we have developed a new instrument with which we can capture and directly manipulate individual myosin subfragment-1 molecules using a scanning probe. Single subfragment-1 molecules can be visualized by using a fluorescent label. The data that we obtain using this technique are consistent with myosin moving along an actin filament with single mechanical steps of approximately 5.3 nanometres; groups of two to five rapid steps in succession often produce displacements of 11 to 30 nanometres. This multiple stepping is produced by a single myosin head during just one biochemical cycle of ATP hydrolysis.Keywords
This publication has 48 references indexed in Scilit:
- Molecular motors: structural adaptations to cellular functionsNature, 1997
- Actomyosin interaction in striated musclePhysiological Reviews, 1997
- X-ray Structures of the Myosin Motor Domain of Dictyostelium discoideum Complexed with MgADP.cntdot.BeFx and MgADP.cntdot.AlF4-Biochemistry, 1995
- How molecular motors workNature, 1994
- Structure of the actin-myosin complex and its implications for muscle contractionScience, 1993
- Three-dimensional structure of myosin subfragment-1: a molecular motorScience, 1993
- Atomic structure of the actin: DNase I complexNature, 1990
- Force measurements by micromanipulation of a single actin filament by glass needlesNature, 1988
- Proposed Mechanism of Force Generation in Striated MuscleNature, 1971
- The Mechanism of Muscular ContractionScience, 1969