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Analysis of flexural rigidity of actin filaments propelled by surface adsorbed myosin motors.

Bengtsson E, Persson M, Månsson A - Cytoskeleton (Hoboken) (2013)

Bottom Line: Actin filaments are central components of the cytoskeleton and the contractile machinery of muscle.The filaments are known to exist in a range of conformational states presumably with different flexural rigidity and thereby different persistence lengths.Our results analyze the approaches proposed previously to measure the persistence length from the statistics of the winding paths of actin filaments that are propelled by surface-adsorbed myosin motor fragments in the in vitro motility assay.

View Article: PubMed Central - PubMed

Affiliation: Faculty of Health and Life Sciences, Linnaeus University, Kalmar, Sweden.

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Fit of single exponential decay function to the cosine correlation function where the latter is based on experimental or simulated data. (A) Experimental data (velocity: 9.27 ± 0.35 µm s−1, mean ± 95% CI; frame rate 5 s−1). (B) Simulated data (velocity: 10 µm·s−1; frame rate 10 s−1). Insets: Relative frequency distribution of angular changes between subsequent measurements.
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fig01: Fit of single exponential decay function to the cosine correlation function where the latter is based on experimental or simulated data. (A) Experimental data (velocity: 9.27 ± 0.35 µm s−1, mean ± 95% CI; frame rate 5 s−1). (B) Simulated data (velocity: 10 µm·s−1; frame rate 10 s−1). Insets: Relative frequency distribution of angular changes between subsequent measurements.

Mentions: Monte-Carlo simulations were performed to analyze critical factors in path persistence length measurements. The simulations have appreciable advantages over experimental data for this purpose as an unambiguous theoretical persistence length (LPtheor) can be defined. The similarity between simulated and experimental data based on 500 and 300 independent paths, respectively, are illustrated in Fig. 1. These data were simulated with LPtheor = 10 µm, compared to experimental data with LP ≈ 11.52 ± 0.46 µm (from fit of Eq. 1).


Analysis of flexural rigidity of actin filaments propelled by surface adsorbed myosin motors.

Bengtsson E, Persson M, Månsson A - Cytoskeleton (Hoboken) (2013)

Fit of single exponential decay function to the cosine correlation function where the latter is based on experimental or simulated data. (A) Experimental data (velocity: 9.27 ± 0.35 µm s−1, mean ± 95% CI; frame rate 5 s−1). (B) Simulated data (velocity: 10 µm·s−1; frame rate 10 s−1). Insets: Relative frequency distribution of angular changes between subsequent measurements.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4230416&req=5

fig01: Fit of single exponential decay function to the cosine correlation function where the latter is based on experimental or simulated data. (A) Experimental data (velocity: 9.27 ± 0.35 µm s−1, mean ± 95% CI; frame rate 5 s−1). (B) Simulated data (velocity: 10 µm·s−1; frame rate 10 s−1). Insets: Relative frequency distribution of angular changes between subsequent measurements.
Mentions: Monte-Carlo simulations were performed to analyze critical factors in path persistence length measurements. The simulations have appreciable advantages over experimental data for this purpose as an unambiguous theoretical persistence length (LPtheor) can be defined. The similarity between simulated and experimental data based on 500 and 300 independent paths, respectively, are illustrated in Fig. 1. These data were simulated with LPtheor = 10 µm, compared to experimental data with LP ≈ 11.52 ± 0.46 µm (from fit of Eq. 1).

Bottom Line: Actin filaments are central components of the cytoskeleton and the contractile machinery of muscle.The filaments are known to exist in a range of conformational states presumably with different flexural rigidity and thereby different persistence lengths.Our results analyze the approaches proposed previously to measure the persistence length from the statistics of the winding paths of actin filaments that are propelled by surface-adsorbed myosin motor fragments in the in vitro motility assay.

View Article: PubMed Central - PubMed

Affiliation: Faculty of Health and Life Sciences, Linnaeus University, Kalmar, Sweden.

Show MeSH
Related in: MedlinePlus