ArticleBiophysical journal2008
Orientation of the essential light chain region of myosin in relaxed, active, and rigor muscle.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Myosin lever arm orientation in muscle determined with high angular resolution using bifunctional spin labels.The Journal of general physiology · 2019Article
- Chemical Crosslinking Mass Spectrometry Analysis of Protein Conformations and Supercomplexes in Heart Tissue.Cell systems · 2018Article
- Amplitude of the actomyosin power stroke depends strongly on the isoform of the myosin essential light chain.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Orientation of the N-terminal lobe of the myosin regulatory light chain in skeletal muscle fibers.Biophysical journal · 2012Article
- Structural and functional aspects of the myosin essential light chain in cardiac muscle contraction.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011Article
- A molecular model of phosphorylation-based activation and potentiation of tarantula muscle thick filaments.Journal of molecular biology · 2011Article
- Response of rigor cross-bridges to stretch detected by fluorescence lifetime imaging microscopy of myosin essential light chain in skeletal muscle fibers.The Journal of biological chemistry · 2011Article
- Visualizing key hinges and a potential major source of compliance in the lever arm of myosin.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Structure and dynamics of the kinesin-microtubule interaction revealed by fluorescence polarization microscopy.Methods in cell biology · 2010Review
- Site-directed spectroscopic probes of actomyosin structural dynamics.Annual review of biophysics · 2009Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The orientation of the ELC region of myosin in skeletal muscle was determined by polarized fluorescence from ELC mutants in which pairs of introduced cysteines were cross-linked by BSR. The purified ELC-BSRs were exchanged for native ELC in demembranated fibers from rabbit psoas muscle using a trifluoperazine-based protocol that preserved fiber function. In the absence of MgATP (in rigor) the ELC orientation distribution was narrow; in terms of crystallographic structures of the myosin head, the LCD long axis linking heavy-chain residues 707 and 843 makes an angle (beta) of 120-125 degrees with the filament axis. This is approximately 30 degrees larger than the broader distribution determined previously from RLC probes, suggesting that, relative to crystallographic structures, the LCD is bent between its ELC and RLC regions in rigor muscle. The ELC orientation distribution in relaxed muscle had two broad peaks with beta approximately 70 degrees and approximately 110 degrees, which may correspond to the two head regions of each myosin molecule, in contrast with the single broad distribution of the RLC region in relaxed muscle. During isometric contraction the ELC orientation distribution peaked at beta approximately 105 degrees , similar to that determined previously for the RLC region.
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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.