### 抄録

By dynamic light scattering, the intensity autocorrelation unction, G^{2}(τ) = B[1+β|g^{1}(τ)|^{2}],was obtained over the scattering angles (θ) from 30 to 130° in steps of 10° for semidilute solutions of muscle F-actin and of F-actin complexed with heavy meromyosin in the absence of ATP (acto-HMM), where B is the baseline and β a constant. The main findings were: (1) A 0.5 mg/ml F-actin solution gave nonreproducible spectra at θ ≦ 40° but quite reproducible spectra at θ ≧ 50°, with β = 0.9-0.8 at all θ values. Nonreproducibility of spectra at low θ values was concluded to be due to restricted motions of very long filaments confined in cages or zig- zag tubing formed by a major fraction of filaments, where the very long filaments were those at a distant tail of an exponential length distribution and the major fraction of filaments were those with lengths around L_{n}-2L_{n}, L_{n} being the number-average length. Spectral widths were compared with theoretical ones for rigid rods averaged over the length distribution with L_{n} = 900 nm, and were suggested to be largely contributed at high θ values from bending motions of filaments. (2) Acto-HMM solutions at 0.5 mg/ml F- actin and at weight ratios of HMM to F-actin of 0.5-2 gave spectra which, with respect to θ, behaved very similarly to those of F-actin alone. The spectral widths, however, drastically decreased with the weight ratio up to unity and stayed virtually constant above unity. In contrast to a previous study (F.D. Carlson and A.B. Fraser, J. Mol. Biol. 89 (1974) 273), β values of acto-HMM were as large as those of F- actin alone. Acto-HMM was concluded to travel a distance far greater than 1/K with a mobility smaller than that of F-actin, where K = ( 4iπ/λ) sin(θ/2), λ being the wavelength of light in the medium. These results suggest that acto-HMM gels are very soft even though they did not pour from an inverted cell. Based on several intuitive models which give a mutual relationship between the β value and modes of motions of scatterers, we discuss the restricted motions responsible for nonreproducibility of spectra at low angles and large β values of acto-HMM gels at all θ values and weight ratios so far studied.

元の言語 | English |
---|---|

ページ（範囲） | 211-224 |

ページ数 | 14 |

ジャーナル | Biophysical Chemistry |

巻 | 27 |

発行部数 | 3 |

DOI | |

出版物ステータス | Published - 1987 |

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### ASJC Scopus subject areas

- Biochemistry
- Biophysics
- Physical and Theoretical Chemistry

### これを引用

*Biophysical Chemistry*,

*27*(3), 211-224. https://doi.org/10.1016/0301-4622(87)80060-1

**Dynamic light-scattering study of muscle F-actin. II.** / Fujime, Satoru; Takasaki-Ohsita, Michiho; Ishiwata, Shin'ichi.

研究成果: Article

*Biophysical Chemistry*, 巻. 27, 番号 3, pp. 211-224. https://doi.org/10.1016/0301-4622(87)80060-1

}

TY - JOUR

T1 - Dynamic light-scattering study of muscle F-actin. II

AU - Fujime, Satoru

AU - Takasaki-Ohsita, Michiho

AU - Ishiwata, Shin'ichi

PY - 1987

Y1 - 1987

N2 - By dynamic light scattering, the intensity autocorrelation unction, G2(τ) = B[1+β|g1(τ)|2],was obtained over the scattering angles (θ) from 30 to 130° in steps of 10° for semidilute solutions of muscle F-actin and of F-actin complexed with heavy meromyosin in the absence of ATP (acto-HMM), where B is the baseline and β a constant. The main findings were: (1) A 0.5 mg/ml F-actin solution gave nonreproducible spectra at θ ≦ 40° but quite reproducible spectra at θ ≧ 50°, with β = 0.9-0.8 at all θ values. Nonreproducibility of spectra at low θ values was concluded to be due to restricted motions of very long filaments confined in cages or zig- zag tubing formed by a major fraction of filaments, where the very long filaments were those at a distant tail of an exponential length distribution and the major fraction of filaments were those with lengths around Ln-2Ln, Ln being the number-average length. Spectral widths were compared with theoretical ones for rigid rods averaged over the length distribution with Ln = 900 nm, and were suggested to be largely contributed at high θ values from bending motions of filaments. (2) Acto-HMM solutions at 0.5 mg/ml F- actin and at weight ratios of HMM to F-actin of 0.5-2 gave spectra which, with respect to θ, behaved very similarly to those of F-actin alone. The spectral widths, however, drastically decreased with the weight ratio up to unity and stayed virtually constant above unity. In contrast to a previous study (F.D. Carlson and A.B. Fraser, J. Mol. Biol. 89 (1974) 273), β values of acto-HMM were as large as those of F- actin alone. Acto-HMM was concluded to travel a distance far greater than 1/K with a mobility smaller than that of F-actin, where K = ( 4iπ/λ) sin(θ/2), λ being the wavelength of light in the medium. These results suggest that acto-HMM gels are very soft even though they did not pour from an inverted cell. Based on several intuitive models which give a mutual relationship between the β value and modes of motions of scatterers, we discuss the restricted motions responsible for nonreproducibility of spectra at low angles and large β values of acto-HMM gels at all θ values and weight ratios so far studied.

AB - By dynamic light scattering, the intensity autocorrelation unction, G2(τ) = B[1+β|g1(τ)|2],was obtained over the scattering angles (θ) from 30 to 130° in steps of 10° for semidilute solutions of muscle F-actin and of F-actin complexed with heavy meromyosin in the absence of ATP (acto-HMM), where B is the baseline and β a constant. The main findings were: (1) A 0.5 mg/ml F-actin solution gave nonreproducible spectra at θ ≦ 40° but quite reproducible spectra at θ ≧ 50°, with β = 0.9-0.8 at all θ values. Nonreproducibility of spectra at low θ values was concluded to be due to restricted motions of very long filaments confined in cages or zig- zag tubing formed by a major fraction of filaments, where the very long filaments were those at a distant tail of an exponential length distribution and the major fraction of filaments were those with lengths around Ln-2Ln, Ln being the number-average length. Spectral widths were compared with theoretical ones for rigid rods averaged over the length distribution with Ln = 900 nm, and were suggested to be largely contributed at high θ values from bending motions of filaments. (2) Acto-HMM solutions at 0.5 mg/ml F- actin and at weight ratios of HMM to F-actin of 0.5-2 gave spectra which, with respect to θ, behaved very similarly to those of F-actin alone. The spectral widths, however, drastically decreased with the weight ratio up to unity and stayed virtually constant above unity. In contrast to a previous study (F.D. Carlson and A.B. Fraser, J. Mol. Biol. 89 (1974) 273), β values of acto-HMM were as large as those of F- actin alone. Acto-HMM was concluded to travel a distance far greater than 1/K with a mobility smaller than that of F-actin, where K = ( 4iπ/λ) sin(θ/2), λ being the wavelength of light in the medium. These results suggest that acto-HMM gels are very soft even though they did not pour from an inverted cell. Based on several intuitive models which give a mutual relationship between the β value and modes of motions of scatterers, we discuss the restricted motions responsible for nonreproducibility of spectra at low angles and large β values of acto-HMM gels at all θ values and weight ratios so far studied.

KW - Dynamic light scattering

KW - F-Actin

KW - Filament flexibility

KW - Heavy meromyosin

KW - Semidilute solution

UR - http://www.scopus.com/inward/record.url?scp=0023411102&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023411102&partnerID=8YFLogxK

U2 - 10.1016/0301-4622(87)80060-1

DO - 10.1016/0301-4622(87)80060-1

M3 - Article

C2 - 3663844

AN - SCOPUS:0023411102

VL - 27

SP - 211

EP - 224

JO - Biophysical Chemistry

JF - Biophysical Chemistry

SN - 0301-4622

IS - 3

ER -