TY - JOUR

T1 - Dynamic light scattering study of muscle f-actin

AU - Fujime, Satoru

AU - Ishiwata, Shin'ichi

AU - Maeda, Tadakazu

PY - 1984

Y1 - 1984

N2 - By use of digital autocorrelation and fast Fourier methods, dynamic light-scattering studies of in vitro reconstituted muscle F-actin were made over a wide range of concentrations. 0.01-2 mg ml F-actin. Measurements of correlation function [g1(t)]2 showed that a transition from a dilute to a semidilute regime for the Brownian motions of filaments occurred at around 0.3 mg ml F-actin. Beyond this concentration, profiles of successively measured [g1(t)]2 showed very poor reproducibility. This resulted from the existence of very slow components, which could not be measured with a high statistical accuracy even for a measuring time of 3600 s/run. On the other hand, subtraction of these components automatically by an electronic circuit, [g-1(t)]2, or by computer processing, [g1(t)]2, resulted in a fairly good reproducibility of the profies, The decay c of [g-1(t)]2 (and [g-1(t)]2) were very similar to those of [g1(t)]2 for dilute solutions. A theoret which could account for the above situation. The time sequence {n(t,T)} of photoelectron counts at a sampling time T of light scattered from semidilute solutions of F-actin was stored on magnetic tapes, and both power spectra S̄(f) and correlation functions [g-1(t)]2 were computed by taking the ensemble average over many short records with duration 1024T. Since both S̄(f and [g-1(t)]2 lacked frequency components lower than 1 (2048T) Hz. their profiles were highly reproducible. An of S̄(f) confirmed our earlier results which had shown an apparent contradiction to later results by a correlation method. A comparison of S̄(f) and [g-1(t)]2 based on the same {n(t,T)} clarified the reasons why the bandwidth Γ of S̄( differed from the bandwidth \ ̄gG of [g1(t)]2 and [g-1(t)]2. The temperature dependence of Γ suggested that F-actin flexible and that the flexibility parameter would change with temperature.

AB - By use of digital autocorrelation and fast Fourier methods, dynamic light-scattering studies of in vitro reconstituted muscle F-actin were made over a wide range of concentrations. 0.01-2 mg ml F-actin. Measurements of correlation function [g1(t)]2 showed that a transition from a dilute to a semidilute regime for the Brownian motions of filaments occurred at around 0.3 mg ml F-actin. Beyond this concentration, profiles of successively measured [g1(t)]2 showed very poor reproducibility. This resulted from the existence of very slow components, which could not be measured with a high statistical accuracy even for a measuring time of 3600 s/run. On the other hand, subtraction of these components automatically by an electronic circuit, [g-1(t)]2, or by computer processing, [g1(t)]2, resulted in a fairly good reproducibility of the profies, The decay c of [g-1(t)]2 (and [g-1(t)]2) were very similar to those of [g1(t)]2 for dilute solutions. A theoret which could account for the above situation. The time sequence {n(t,T)} of photoelectron counts at a sampling time T of light scattered from semidilute solutions of F-actin was stored on magnetic tapes, and both power spectra S̄(f) and correlation functions [g-1(t)]2 were computed by taking the ensemble average over many short records with duration 1024T. Since both S̄(f and [g-1(t)]2 lacked frequency components lower than 1 (2048T) Hz. their profiles were highly reproducible. An of S̄(f) confirmed our earlier results which had shown an apparent contradiction to later results by a correlation method. A comparison of S̄(f) and [g-1(t)]2 based on the same {n(t,T)} clarified the reasons why the bandwidth Γ of S̄( differed from the bandwidth \ ̄gG of [g1(t)]2 and [g-1(t)]2. The temperature dependence of Γ suggested that F-actin flexible and that the flexibility parameter would change with temperature.

KW - Dynamic light scattering

KW - F-Actin

KW - Fast Fourier method

KW - Filament flexibility

KW - Semidilute solution

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U2 - 10.1016/0301-4622(84)80001-0

DO - 10.1016/0301-4622(84)80001-0

M3 - Article

C2 - 6487741

AN - SCOPUS:0021188467

VL - 20

SP - 1

EP - 21

JO - Biophysical Chemistry

JF - Biophysical Chemistry

SN - 0301-4622

IS - 1-2

ER -