ArticleBiophysical journal2015
Stabilizing the central part of tropomyosin increases the bending stiffness of the thin filament.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Effects of Cardiomyopathic Mutations on the Cytoplasmic Tropomyosin Isoform Tpm1.7.Molecules (Basel, Switzerland) · 2026Article
- Functional and Structural Properties of Cytoplasmic Tropomyosin Isoforms Tpm1.8 and Tpm1.9.International journal of molecular sciences · 2024Article
- Structural and Functional Peculiarities of Cytoplasmic Tropomyosin Isoforms, the Products ofInternational journal of molecular sciences · 2021Article
- Functional outcomes of structural peculiarities of striated muscle tropomyosin.Journal of muscle research and cell motility · 2020Review
- Optical Tweezers Approaches for Probing Multiscale Protein Mechanics and Assembly.Frontiers in molecular biosciences · 2020Review
- Effects of an Interchain Disulfide Bond on Tropomyosin Structure: A Molecular Dynamics Study.International journal of molecular sciences · 2018Article
- Cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin.Journal of muscle research and cell motility · 2017Article
- The Relaxation Properties of Myofibrils Are Compromised by Amino Acids that Stabilize α-Tropomyosin.Biophysical journal · 2017Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A two-beam optical trap was used to measure the bending stiffness of F-actin and reconstructed thin filaments. A dumbbell was formed by a filament segment attached to two beads that were held in the two optical traps. One trap was static and held a bead used as a force transducer, whereas an acoustooptical deflector moved the beam holding the second bead, causing stretch of the dumbbell. The distance between the beads was measured using image analysis of micrographs. An exact solution to the problem of bending of an elastic filament attached to two beads and subjected to a stretch was used for data analysis. Substitution of noncanonical residues in the central part of tropomyosin with canonical ones, G126R and D137L, and especially their combination, caused an increase in the bending stiffness of the thin filaments. The data confirm that the effect of these mutations on the regulation of actin-myosin interactions may be caused by an increase in tropomyosin stiffness.
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Registered trials
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