Fluctuation Correlation in the Sliding Movement Generated by Protein Motors In Vitro

Tawada, Katsuhisa; Toyoda, Masahiro; Imafuku, Yasuhiro; Yamada, Akira

doi:10.1007/978-1-4684-6039-1_6

Cited by 2 publications

(5 citation statements)

References 7 publications

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“…The proper cutoff frequency for the smoothing was chosen by examining the fast Fourier transform power spectra of the time series. The smoothing does not significantly affect either the fluctuation or the steady characteristics inherent to the filament sliding movements by protein motors in vitro as we have shown by a Monte Carlo study (Imafuku et al, 1995).…”

Section: Smoothing Of the Trajectoriesmentioning

confidence: 55%

“…This places constraint on the possible molecular mechanisms of the sliding movement in vitro as will be discussed below. Some of these results have been briefly reported to the Seventh Biophysical Discussions on Molecular Motors (Tawada et al, 1995).…”

Section: Introductionmentioning

confidence: 85%

“…where o-r is the variance of the distance measurement errors (Bevington and Robinson, 1992;Imafuku et al, 1995;Qian et al, 1991). As the linear sliding distance is given by the distance between two positions on the computer screen, the variance of the distance measurement errors in Eq.…”

Section: Data Collectionmentioning

confidence: 99%

“…There is a lag in the graph at small time intervals. The lag is a result of the smoothing with low-pass filtering (Imafuku et al, 1995). After the lag, there is a linear portion in the graph, as shown by the line.…”

Section: Smoothing Of the Trajectoriesmentioning

confidence: 99%

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Fluctuation in the microtubule sliding movement driven by kinesin in vitro

Imafuku

Toyoshima

Tawada

1996

Biophysical Journal

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We studied the fluctuation in the translational sliding movement of microtubules driven by kinesin in a motility assay in vitro. By calculating the mean-square displacement deviation from the average as a function of time, we obtained motional diffusion coefficients for microtubules and analyzed the dependence of the coefficients on microtubule length. Our analyses suggest that 1) the motional diffusion coefficient consists of the sum of two terms, one that is proportional to the inverse of the microtubule length (as the longitudinal diffusion coefficient of a filament in Brownian movement is) and another that is independent of the length, and 2) the length-dependent term decreases with increasing kinesin concentration. This latter term almost vanishes within the length range we studied at high kinesin concentrations. From the length-dependence relationship, we evaluated the friction coefficient for sliding microtubules. This value is much larger than the solvent friction and thus consistent with protein friction. The length independence of the motional diffusion coefficient observed at sufficiently high kinesin concentrations indicates the presence of correlation in the sliding movement fluctuation. This places significant constraint on the possible mechanisms of the sliding movement generation by kinesin motors in vitro.

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Section: Smoothing Of the Trajectoriesmentioning

confidence: 55%

Section: Introductionmentioning

confidence: 85%

Section: Data Collectionmentioning

confidence: 99%

Section: Smoothing Of the Trajectoriesmentioning

confidence: 99%

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Fluctuation in the microtubule sliding movement driven by kinesin in vitro

Imafuku

Toyoshima

Tawada

1996

Biophysical Journal

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“…One is for how a single myosin motor could transform chemical energy stored in an ATP into mechanical one for the sliding movement [1][2][3][4][5][6][7]. One more process is for how each myosin motor could generate mechanical forces in a coordinated manner along the filament [8][9][10][11][12][13][14]. If adjacent actomyosin complexes along the filament are not coordinated with their timing of ATP hydrolysis and the resulting force generation, there must be a considerable amount of mechanical stains or distortions along the filament [15][16][17].…”

Section: Introductionmentioning

confidence: 99%

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Honda

Kikuchi

Hatori

et al. 2002

Journal of Biological Physics

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An actin filament sliding on myosin moleculesdemonstrates both longitudinal distortions and transversal fluctuationswith the linear dimension far exceeding the diameter of an actinmonomer. Local swaying of a single actin filament was identified byreading speckled fluorescent markers attached on the filament. Theaccuracy of reading each speckled marker was about 10.4 nm (r.m.s.).Longitudinal distortions of an actin filament at a low ATP concentrationof 20 μM were as much as 0.5 μm for the average filament lengthof 5.4 μm. The magnitude of transversal fluctuations was as much as60 nm, that was independent of the filament length. Both longitudinaldistortions and transversal fluctuations are suggested to play a pivotalrole for facilitating a smooth sliding movement of an actin filament.

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Fluctuation Correlation in the Sliding Movement Generated by Protein Motors In Vitro

Cited by 2 publications

References 7 publications

Fluctuation in the microtubule sliding movement driven by kinesin in vitro

Fluctuation in the microtubule sliding movement driven by kinesin in vitro

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