| Autor: |
Justin E. Molloy, Alex E. Knight, Jeremy C. Fielden, Rachel E. Farrow |
| Rok vydání: |
2009 |
| Předmět: |
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| DOI: |
10.1016/b978-0-12-374227-8.00001-8 |
| Popis: |
This chapter focuses on the single molecule studies of myosins and specifically research work with myosin II and myosin V. Single molecule studies of actomyosin, the molecular motor system of actin and myosin, have been at the forefront in terms of technology development and applying new and emerging techniques to address highly specific questions of how it works. Much of what we know about the mechanism by which myosin produces force and movement stems from early structural, mechanical, and biochemical studies performed using single muscle fibers from frogs and purified proteins from rabbits. Single molecule approaches have made a major impact in obtaining an increasingly clear picture of how myosin works at the level of molecular rearrangements during the ATPase cycle. Many of these methods are broadly applicable to other fields. The single molecule techniques originally devised to study actomyosin from muscle have opened up an entire field of science that allows biophysicists to make major contributions to our understanding of cell motility and cell biology. In vitro motility assays enable actomyosin motility to be reconstituted from purified component molecules. Rhodamine-phalloidin-labeled actin filaments can be visualized by fluorescence microscopy as they move on a microscope coverslip surface that has been coated with myosin or one of its proteolytic subfragments. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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