ArticleBiophysical journal2005
Persistence length of titin from rabbit skeletal muscles measured with scattering and microrheology techniques.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 22 citations in OpenAlex.
- Detecting the Biopolymer Behavior of Graphene Nanoribbons in Aqueous Solution.Scientific reports · 2016Article
- Microrheology with optical tweezers: measuring the relative viscosity of solutions 'at a glance'.Scientific reports · 2015Article
- Beyond lamins other structural components of the nucleoskeleton.Methods in cell biology · 2010Review
- Roles of titin in the structure and elasticity of the sarcomere.Journal of biomedicine & biotechnology · 2010Review
- Comparative biomechanics of thick filaments and thin filaments with functional consequences for muscle contraction.Journal of biomedicine & biotechnology · 2010Review
- A regular pattern of Ig super-motifs defines segmental flexibility as the elastic mechanism of the titin chain.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Poly-Ig tandems from I-band titin share extended domain arrangements irrespective of the distinct features of their modular constituents.Journal of muscle research and cell motility · 2005Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The persistence length of titin from rabbit skeletal muscles was measured using a combination of static and dynamic light scattering, and neutron small angle scattering. Values of persistence length in the range 9-16 nm were found for titin-II, which corresponds to mainly physiologically inelastic A-band part of the protein, and for a proteolytic fragment with 100-nm contour length from the physiologically elastic I-band part. The ratio of the hydrodynamic radius to the static radius of gyration indicates that the proteins obey Gaussian statistics typical of a flexible polymer in a -solvent. Furthermore, measurements of the flexibility as a function of temperature demonstrate that titin-II and the I-band titin fragment experience a similar denaturation process; unfolding begins at 318 K and proceeds in two stages: an initial gradual 50% change in persistence length is followed by a sharp unwinding transition at 338 K. Complementary microrheology (video particle tracking) measurements indicate that the viscoelasticity in dilute solution behaves according to the Flory/Fox model, providing a value of the radius of gyration for titin-II (63 +/- 1 nm) in agreement with static light scattering and small angle neutron scattering results.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.