ArticleBiophysical journal2000
The effect of polyethylene glycol on the mechanics and ATPase activity of active muscle fibers.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
The trial behind it
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Thick-to-thin filament surface distance modulates cross-bridge kinetics in Drosophila flight muscle.Biophysical journal · 2012Article
- Pre-power stroke cross bridges contribute to force during stretch of skeletal muscle myofibrils.Proceedings. Biological sciences · 2008Article
- Dynamics of the nucleotide pocket of myosin measured by spin-labeled nucleotides.Biophysical journal · 2007Article
- Structural characterization of the binding of Myosin*ADP*Pi to actin in permeabilized rabbit psoas muscle.Biophysical journal · 2006Article
- The force exerted by a muscle cross-bridge depends directly on the strength of the actomyosin bond.Biophysical journal · 2004Article
- Force enhancement by PEG during ramp stretches of skeletal muscle.Journal of muscle research and cell motility · 2003Article
- Characterization of the cross-bridge force-generating step using inorganic phosphate and BDM in myofibrils from rabbit skeletal muscles.The Journal of physiology · 2002Article
- Dimethyl sulphoxide enhances the effects of P(i) in myofibrils and inhibits the activity of rabbit skeletal muscle contractile proteins.The Biochemical journal · 2001Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
We have used polyethylene glycol (PEG) to perturb the actomyosin interaction in active skinned muscle fibers. PEG is known to potentiate protein-protein interactions, including the binding of myosin to actin. The addition of 5% w/v PEG (MW 300 or 4000) to active fibers increased fiber tension and decreased shortening velocity and ATPase activity, all by 25-40%. Variation in [ADP] or [ATP] showed that the addition of PEG had little effect on the dissociation of the cross-bridge at the end of the power stroke. Myosin complexed with ADP and the phosphate analog V(i) or AlF(4) binds weakly to actin and is an analog of a pre-power-stroke state. PEG substantially enhances binding of these states both in active fibers and in solution. Titration of force with increasing [P(i)] showed that PEG increased the free energy available to drive the power stroke by about the same amount as it increased the free energy available from the formation of the actomyosin bond. Thus PEG potentiates the binding of myosin to actin in active fibers, and it provides a method for enhancing populations of some states for structural or mechanical studies, particularly those of the normally weakly bound transient states that precede the power stroke.
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What OpenQuestion holds
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.