Abstract
Muscle contraction results from ATP-dependent sliding between actin filaments and S1 domain of myosin, but its molecular mechanism of chemomechanical energy transformation is still elusive despite decades of extensive research. There were three major breakthroughs in this field during the last few years, however; recombinant myosin technology, monomolecular in vitro motility assay, and atomic structure of S1. This article briefly reviews what is currently under dispute in this field, and introduces how molecular biologists, with these new tools in hand, are approaching those questions.
Original language | English |
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Pages (from-to) | 1-11 |
Number of pages | 11 |
Journal | Materials Science and Engineering C |
Volume | 2 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 1994 Dec |
Externally published | Yes |
Keywords
- Atomic structure
- Motor research
- Myosin
ASJC Scopus subject areas
- Materials Science(all)
- Condensed Matter Physics
- Mechanics of Materials
- Mechanical Engineering