ArticleEuropean biophysics journal : EBJ2015
The lifetime of the actomyosin complex in vitro under load corresponding to stretch of contracting muscle.
Article in European biophysics journal : EBJ, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Review
- Carbonylation of atrial myosin prolongs its interaction with actin.European biophysics journal : EBJ · 2018Article
- Cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin.Journal of muscle research and cell motility · 2017Article
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Authors and funding
4 authors.
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Abstract
During eccentric contraction, muscle is lengthening so that the actin-myosin cross-bridges bear a load that exceeds the force they generate during isometric contraction. Using the optical trap technique, we simulated eccentric contraction at the single molecule level and investigated the effect of load on the skeletal actomyosin lifetime at different ATP concentrations. The range of the loads was up to 17 pN above the isometric level. We found that the frequency distribution of the lifetime of the actin-bound state of the myosin molecule was biphasic: it quickly rose and then decreased slowly. The rate of the slow phase of this distribution increased with both the load and the ATP concentration. The fast phase accelerated sharply with the load, but it was independent of ATP concentration. The presence of the fast phase demonstrates that some transition(s) in the actomyosin complex occur before the myosin head becomes able to bind ATP and detach from actin. Its high sensitivity to the load indicates that the transition is load-dependent.
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