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3-DIMENSIONAL STRUCTURE OF MYOSIN SUBFRAGMENT-1 - A MOLECULAR MOTOR
Author(s): RAYMENT I, RYPNIEWSKI WR, SCHMIDTBASE K, SMITH R, TOMCHICK DR, BENNING MM, WINKELMANN DA, WESENBERG G, HOLDEN HM
Source: SCIENCE    Volume: 261    Issue: 5117    Pages: 50-58    Published: JUL 2 1993  
Times Cited: 1,476     References: 74     
Abstract: Directed movement is a characteristic of many living organisms and occurs as a result of the transformation of chemical energy into mechanical energy. Myosin is one of three families of molecular motors that are responsible for cellular motility. The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described. This structure of a molecular motor was determined by single crystal x-ray diffraction. The data provide a structural framework for understanding the molecular basis of motility.
Document Type: Article
Language: English
Reprint Address: RAYMENT, I (reprint author), UNIV WISCONSIN, DEPT BIOCHEM, 1710 UNIV AVE, MADISON, WI 53705 USA
Addresses:
1. UNIV WISCONSIN, INST ENZYME RES, MADISON, WI 53705 USA
2. ROBERT WOOD JOHNSON MED SCH, DEPT PATHOL, PISCATAWAY, NJ 08854 USA
Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005
Subject Category: Multidisciplinary Sciences
IDS Number: LK434
ISSN: 0036-8075
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