ArticleBiophysical journal1998
Behavior of N-phenylmaleimide-reacted muscle fibers in magnesium-free rigor solution.
Article in Biophysical journal, 1998. 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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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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Who cites it
3 citing papers in PubMed.
- Structural characterization of weakly attached cross-bridges in the A*M*ATP state in permeabilized rabbit psoas muscle.Biophysical journal · 2002Article
- A model of cross-bridge attachment to actin in the A*M*ATP state based on x-ray diffraction from permeabilized rabbit psoas muscle.Biophysical journal · 2002Article
- The M.ADP.Pi state is required for helical order in the thick filaments of skeletal muscle.Biophysical journal · 1999Article
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Authors and funding
3 authors.
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Abstract
Using x-ray diffraction and mechanical stiffness, the response of N-phenylmaleimide (NPM)-reacted cross-bridges to solutions containing different amounts of ATP and Mg2+ has been studied. In relaxing solution containing greater than millimolar amounts of ATP and Mg2+, NPM-treated muscle fibers give x-ray diffraction patterns and stiffness records, which are nearly indistinguishable from those of untreated relaxed fibers. In a solution devoid of added ATP, but with Mg2+ (rigor(+Mg) solution), the muscle fibers still give x-ray diffraction patterns and mechanical responses characteristic of relaxed muscle. The new finding reported here is that in a solution devoid of both ATP and Mg2+ (rigor(-Mg) solution containing EDTA with no added ATP), NPM-reacted cross-bridges do give rigor-like behavior. This is the first report that NPM-reacted cross-bridges, at least in the presence of EDTA, are capable of going into a strongly binding conformation.
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