Myosin-induced volume increase of the hyper-mobile water surrounding actin filaments

Makoto Suzuki, Syed Rashel Kabir, Md Shahjahan Parvez Siddique, Umme Salma Nazia, Takashi Miyazaki, Takao Kodama

Research output: Contribution to journalArticlepeer-review

39 Citations (Scopus)


Microwave dielectric spectroscopy can measure the rotational mobility of water molecules that hydrate proteins and the hydration-shell volume. Using this technique, we have recently shown that apart from typical hydrating water molecules with lowered mobility there are other water molecules around the actin filaments (F-actin) which have a much higher mobility than that of bulk water [Biophys. J. 85 (2003) 3154]. We report here that the volume of this water component (hyper-mobile water) markedly increases without significant change of the volume of the ordinary hydration shell when the myosin motor-domain (S1, myosin subfragment-1) binds to F-actin. No hyper-mobile component was found in the hydration shell of S1 itself. The present results strongly suggest that the solvent space around S1 bound to F-actin is diffusionally asymmetric, which supports our model of force generation by actomyosin proposed previously [op. cit.].

Original languageEnglish
Pages (from-to)340-346
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 2004 Sep 10


  • Actin filament
  • Actomyosin
  • Brownian ratchet
  • Hyper-mobile water
  • Linear motor mechanism
  • Microwave dielectric spectroscopy
  • Negative hydration
  • Protein hydration
  • Urea hydration
  • Water structure breaker

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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