Three recent breakthroughs in molecular motor research: recombinant myosin, monomolecular in vitro motility assay and atomic structure of S1

Taro Q.P. Uyeda*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

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 languageEnglish
Pages (from-to)1-11
Number of pages11
JournalMaterials Science and Engineering C
Volume2
Issue number1-2
DOIs
Publication statusPublished - 1994 Dec
Externally publishedYes

Keywords

  • Atomic structure
  • Motor research
  • Myosin

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Mechanics of Materials
  • Mechanical Engineering

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