ArticleBiophysical journal2010
Monitoring the structural behavior of troponin and myoplasmic free Ca2+ concentration during twitch of frog skeletal muscle.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Bacterial Amyloids as Hubs for Nucleic Acid Interactions: Implications and Mechanisms.International journal of molecular sciences · 2025Review
- The Transient Mechanics of Muscle Require Only a Single Force-Producing Cross-Bridge State and a 100 Å Working Stroke.Biology · 2020Article
- Crossbridge Recruitment Capacity of Wild-Type and Hypertrophic Cardiomyopathy-Related Mutant Troponin-T Evaluated by X-ray Diffraction and Mechanical Study of Cardiac Skinned Fibers.International journal of molecular sciences · 2020Article
- Synchrotron radiation X-ray diffraction studies on muscle: past, present, and future.Biophysical reviews · 2019Review
- Regulation of Contraction by the Thick Filaments in Skeletal Muscle.Biophysical journal · 2017Review
- Modeling CaFrontiers in physiology · 2016Article
- Structural dynamics of troponin during activation of skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Sarcomere-length dependence of myosin filament structure in skeletal muscle fibres of the frog.The Journal of physiology · 2014Article
- High-speed detector for time-resolved diffraction studies.Journal of physics. Conference series · 2013Article
- Motion of myosin head domains during activation and force development in skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- X-ray fiber diffraction modeling of structural changes of the thin filament upon activation of live vertebrate skeletal muscles.Biophysics (Nagoya-shi, Japan) · 2010Article
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interaction of troponin molecules on the thin filament with Ca(2+) plays a key role in regulating muscle contraction. To characterize the structural changes of troponin caused by Ca(2+) and crossbridge formation, we recorded the small-angle x-ray intensity and the myoplasmic free Ca(2+) concentration using fluo-3 AM in the same frog skeletal muscle during twitch elicited by a single electrical pulse at 16 degrees C. In an overstretched muscle, the intensity of the meridional reflection from troponin at 1/38.5 nm(-1) began to change at 4 ms after the stimulus, reached a peak at 10 ms, and returned to the resting level with a halftime of 25 ms. The concentration of troponin-bound Ca(2+) began to increase at 1-2 ms after the stimulus, reached a peak at 5 ms, and returned to the resting level with a halftime of 40 ms, indicating that troponin begins to change conformation only after a sizable amount of Ca(2+) has bound to it, and returns to the resting structure even when there is still some bound Ca(2+). In a muscle with a filament overlap, crossbridge formation appears to slow down Ca(2+) release from troponin and have a large effect on its conformation.
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