ArticleBiochemistry1998
Microsecond rotational dynamics of spin-labeled myosin regulatory light chain induced by relaxation and contraction of scallop muscle.
Article in Biochemistry, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 33 citations in OpenAlex.
- Dynamics of ATP-dependent and ATP-independent steppings of myosin-V on actin: catch-bond characteristics.Journal of the Royal Society, Interface · 2020Article
- A model for the chemomechanical coupling of myosin-V molecular motors.RSC advances · 2019Article
- Three distinct actin-attached structural states of myosin in muscle fibers.Biophysical journal · 2012Article
- Site-directed spectroscopic probes of actomyosin structural dynamics.Annual review of biophysics · 2009Review
- Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Progress in neurobiology · 2008Review
- Orientation of the myosin light chain region by single molecule total internal reflection fluorescence polarization microscopy.Biophysical journal · 2005Article
- Mechanical defects of muscle fibers with myosin light chain mutants that cause cardiomyopathy.Biophysical journal · 2003Article
- Coordination of the two heads of myosin during muscle contraction.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Conformational dynamics of the SH1-SH2 helix in the transition states of myosin subfragment-1.Biophysical journal · 2002Article
- Molecular dynamics simulation of site-directed spin labeling: experimental validation in muscle fibers.Biophysical journal · 2002Article
- Polarized fluorescence depletion reports orientation distribution and rotational dynamics of muscle cross-bridges.Biophysical journal · 2002Article
- Conformational change of the actomyosin complex drives the multiple stepping movement.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Holding two heads together: stability of the myosin II rod measured by resonance energy transfer between the heads.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Changes in actin and myosin structural dynamics due to their weak and strong interactions.Results and problems in cell differentiation · 2002Review
- Actin and temperature effects on the cross-linking of the SH1-SH2 helix in myosin subfragment 1.Biophysical journal · 2000Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
We have used saturation transfer electron paramagnetic resonance (ST-EPR) to study the rotational dynamics of spin-labeled regulatory light chain (RLC) in scallop (Placopecten magellanicus) muscle fibers. The single cysteine (Cys 51) in isolated clam (Mercenaria) RLC was labeled with an indanedione spin label (InVSL). RLC was completely and specifically extracted from scallop striated muscle fibers, eliminating the Ca sensitivity of ATPase activity and isometric force, which were both completely restored by stoichiometric incorporation of labeled RLC. The EPR spectrum of the isolated RLC revealed nanosecond rotational motions within the RLC, which were completely eliminated when the labeled RLC was bound to myosin heads in myofibrils or fibers in rigor. This is the most strongly immobilized RLC-bound probe reported to date and thus offers the most reliable detection of the overall rotational motion of the LC domain. Conventional EPR spectra of oriented fibers indicated essentially complete probe disorder, independent of ATP and Ca, eliminating orientational dependence and thus making this probe ideal for unambiguous measurement of microsecond rotational motions of the LC domain by ST-EPR. ST-EPR spectra of fibers in rigor indicated an effective rotational correlation time (taureff) of 140 +/- 5 microseconds, similar to that observed for the same spin label bound to the catalytic domain. Relaxation by ATP induced microsecond rotational motion (taureff = 70 +/- 4 microseconds), and this motion was slightly slower upon Ca activation of isometric contraction (taureff = 100 +/- 5 microseconds). These motions in relaxation and contraction are similar to, but slower than, the motions previously reported for the same spin label bound to the catalytic domain. These results support a model for force generation involving rotational motion of the LC domain relative to the catalytic domain and dynamic disorder-to-order transitions in both domains.
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