ReviewJournal of muscle research and cell motility2002
Single-molecule measurement of elasticity of serine-, glutamate- and lysine-rich repeats of invertebrate connectin reveals that its elasticity is caused entropically by random coil structure.
Review in Journal of muscle research and cell motility, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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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2 citing papers in PubMed, 9 citations in OpenAlex.
- Giant ankyrin-G: a critical innovation in vertebrate evolution of fast and integrated neuronal signaling.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Pulling single molecules of titin by AFM--recent advances and physiological implications.Pflugers Archiv : European journal of physiology · 2008Review
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6 authors at 1 institution in 1 country.
Funding
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Abstract
Invertebrate connectin (I-connectin) is a 1960 kDa elastic protein linking the Z line to the tip of the myosin filament in the giant sarcomere of crayfish claw closer muscle (Fukuzawa et al., 2001 EMBO J 20: 4826-4835). I-Connectin can be extended up to 3.5 microns upon stretch of giant sarcomeres. There are several extensible regions in I-connectin: two long PEVK regions, one unique sequence region and Ser-, Glu- and Lys-rich 68 residue-repeats called SEK repeats. In the present study, the force measurement of the single recombinant SEK polypeptide containing biotinylated BDTC and GST tags at the N and C termini, respectively, were performed by intermolecular force microscopy (IFM), a refined AFM system. The force vs. extension curves were well fit to the wormlike chain (WLC) model and the obtained persistence length of 0.37 +/- 0.01 nm (n = 11) indicates that the SEK region is a random coil along its full length. This is the first observation of an entropic elasticity of a fully random coil region that contributes to the physiological function of I-connectin.
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