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Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?
Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.ORCID iD: 0000-0002-5889-7792
Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
McGill Univ, Canada.
2018 (English)In: International Journal of Molecular Sciences, ISSN 1422-0067, E-ISSN 1422-0067, Vol. 19, no 7, article id 1863Article, review/survey (Refereed) Published
Abstract [en]

In muscle, but not in single-molecule mechanics studies, actin, myosin and accessory proteins are incorporated into a highly ordered myofilament lattice. In view of this difference we compare results from single-molecule studies and muscle mechanics and analyze to what degree data from the two types of studies agree with each other. There is reasonable correspondence in estimates of the cross-bridge power-stroke distance (7-13 nm), cross-bridge stiffness (similar to 2 pN/nm) and average isometric force per cross-bridge (6-9 pN). Furthermore, models defined on the basis of single-molecule mechanics and solution biochemistry give good fits to experimental data from muscle. This suggests that the ordered myofilament lattice, accessory proteins and emergent effects of the sarcomere organization have only minor modulatory roles. However, such factors may be of greater importance under e.g., disease conditions. We also identify areas where single-molecule and muscle data are conflicting: (1) whether force generation is an Eyring or Kramers process with just one major power-stroke or several sub-strokes; (2) whether the myofilaments and the cross-bridges have Hookean or non-linear elasticity; (3) if individual myosin heads slip between actin sites under certain conditions, e.g.,in lengthening; or (4) if the two heads of myosin cooperate.

Place, publisher, year, edition, pages
MDPI, 2018. Vol. 19, no 7, article id 1863
Keywords [en]
optical tweezers, optical traps, muscle fiber, myofibril, myosin, actin, cross-bridge, mechanochemical model
National Category
Biophysics Biochemistry and Molecular Biology
Research subject
Chemistry, Biochemistry
Identifiers
URN: urn:nbn:se:lnu:diva-77732DOI: 10.3390/ijms19071863ISI: 000442807400042PubMedID: 29941816Scopus ID: 2-s2.0-85049149996OAI: oai:DiVA.org:lnu-77732DiVA, id: diva2:1248040
Available from: 2018-09-13 Created: 2018-09-13 Last updated: 2019-08-29Bibliographically approved

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Månsson, AlfUšaj, MarkoMoretto, Luisa

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