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

doi:10.1016/j.bbrc.2004.07.111

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

ENG - Materials Processing

Research output: Contribution to journal › Article › peer-review

36 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	340-346
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	322
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2004.07.111
Publication status	Published - 2004 Sep 10

Keywords

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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Myosin-induced volume increase of the hyper-mobile water surrounding actin filaments. / Suzuki, Makoto; Kabir, Syed Rashel; Siddique, Md Shahjahan Parvez; Nazia, Umme Salma; Miyazaki, Takashi; Kodama, Takao.

In: Biochemical and Biophysical Research Communications, Vol. 322, No. 1, 10.09.2004, p. 340-346.

Research output: Contribution to journal › Article › peer-review

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abstract = "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.].",

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AU - Miyazaki, Takashi

AU - Kodama, Takao

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