Journal
CELL MOTILITY AND THE CYTOSKELETON
Volume 51, Issue 1, Pages 1-15Publisher
WILEY-LISS
DOI: 10.1002/cm.10014
Keywords
-
Categories
Funding
- NHLBI NIH HHS [HL66157, HL59408, HL54568] Funding Source: Medline
- NIDDK NIH HHS [DK-10113] Funding Source: Medline
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL066157, P01HL059408, R01HL054568] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [F32DK010113] Funding Source: NIH RePORTER
Ask authors/readers for more resources
Optical trapping technology now allows investigators in the motility field to measure the forces generated by single motor molecules. A handful of research groups have exploited this approach to further develop our understanding of the actin-based motor, myosin, an ATPase that is capable of converting chemical energy into mechanical work during a cyclical interaction with filamentous actin. In this regard, myosin-II from muscle is the most well-characterized myosin superfamily member. By combining the data obtained from optical trap assays with that from ensemble biochemical and mechanical assays, this review discusses the fundamental properties of the myosin-II power stroke and, perhaps more significantly, how these properties are governed by this molecule's atomic structure and the biochemical transitions that define its catalytic cycle. (C) 2002 Wiley-Liss, Inc.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available