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Analysis of Flexural Rigidity of Actin Filaments Propelled by Surface Adsorbed Myosin Motors
Faculty of Health and Life Sciences, Linnaeus University, Kalmar, Sweden.
Faculty of Health and Life Sciences, Linnaeus University, Kalmar, Sweden.ORCID iD: 0000-0003-2819-3046
Faculty of Health and Life Sciences, Linnaeus University, Kalmar, Sweden.
2013 (English)In: Cytoskeleton, ISSN 1949-3584, Vol. 70, no 11, p. 718-728Article in journal (Refereed) Published
Abstract [en]

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. Our results suggest that the persistence length of heavy meromyosin propelled actin filaments can be estimated with high accuracy and reproducibility using this approach provided that: (1) the in vitro motility assay experiments are designed to prevent bias in filament sliding directions, (2) at least 200 independent filament paths are studied, (3) the ratio between the sliding distance between measurements and the camera pixel-size is between 4 and 12, (4) the sliding distances between measurements is less than 50% of the expected persistence length, and (5) an appropriate cut-off value is chosen to exclude abrupt large angular changes in sliding direction that are complications, e.g., due to the presence of rigor heads. If the above precautions are taken the described method should be a useful routine part of in vitro motility assays thus expanding the amount of information to be gained from these.

Place, publisher, year, edition, pages
John Wiley & Sons, 2013. Vol. 70, no 11, p. 718-728
Keywords [en]
actin, cytoskeletal filament, Monte-Carlo simulations, molecular motor, F-ACTIN, THERMAL FLUCTUATIONS, DYNAMIC POLYMORPHISM, STRUCTURAL DYNAMICS, ACTOMYOSIN FUNCTION, FORCE MICROSCOPY, FLEXIBILITY, TRANSPORT, MOTILITY, BUNDLES
National Category
Biophysics
Identifiers
URN: urn:nbn:se:oru:diva-99358DOI: 10.1002/cm.21138ISI: 000327310200004PubMedID: 24039103Scopus ID: 2-s2.0-84888199072OAI: oai:DiVA.org:oru-99358DiVA, id: diva2:1663615
Funder
Swedish Research Council, 621-2010-5146Carl Tryggers foundation The Crafoord Foundation
Note

Funding agencies:

Faculty of Natural Sciences and Engineering at Linnaeus University

Faculty of Health and Life Sciences at Linnaeus University

Available from: 2022-06-02 Created: 2022-06-02 Last updated: 2023-12-08Bibliographically approved

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