ArticleBiophysical journal2005
Orientation of the myosin light chain region by single molecule total internal reflection fluorescence polarization microscopy.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 57 citations in OpenAlex.
- Strategy for Generating Giant Unilamellar Vesicles with Tunable Size Using the Modified cDICE Method.ACS synthetic biology · 2025Article
- Self-assembled active actomyosin gels spontaneously curve and wrinkle similar to biological cells and tissues.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Stokes polarimetry-based second harmonic generation microscopy for collagen and skeletal muscle fiber characterization.Lasers in medical science · 2021Article
- Single molecule turnover of fluorescent ATP by myosin and actomyosin unveil elusive enzymatic mechanisms.Communications biology · 2021Article
- Myosin and Other Energy-Transducing ATPases: Structural Dynamics Studied by Electron Paramagnetic Resonance.International journal of molecular sciences · 2020Review
- Enhanced DNA imaging using super-resolution microscopy and simultaneous single-molecule orientation measurements.Optica · 2016Article
- Determining the rotational mobility of a single molecule from a single image: a numerical study.Optics express · 2015Article
- Phosphorylation of myosin regulatory light chain has minimal effect on kinetics and distribution of orientations of cross bridges of rabbit skeletal muscle.American journal of physiology. Regulatory, integrative and comparative physiology · 2014Article
- Breaking the millisecond barrier: single molecule motors wobble to find their next binding sites.Biophysical journal · 2013Article
- Tilting and wobble of myosin V by high-speed single-molecule polarized fluorescence microscopy.Biophysical journal · 2013Article
- Mesoscopic analysis of motion and conformation of cross-bridges.Biophysical reviews · 2012Review
- Orientation and rotational motions of single molecules by polarized total internal reflection fluorescence microscopy (polTIRFM).Cold Spring Harbor protocols · 2012Article
- The 64th Symposium of the Society for General Physiologists: optogenetics and superresolution microscopy take center stage.The Journal of general physiology · 2011Article
- Imaging skeletal muscle using second harmonic generation and coherent anti-Stokes Raman scattering microscopy.Biomedical optics express · 2011Article
- Enhancement of single-molecule fluorescence signals by colloidal silver nanoparticles in studies of protein translation.ACS nano · 2011Article
- Changepoint analysis for single-molecule polarized total internal reflection fluorescence microscopy experiments.Methods in enzymology · 2011Article
- Observing cycling of a few cross-bridges during isometric contraction of skeletal muscle.Cytoskeleton (Hoboken, N.J.) · 2010Article
- Single molecule kinetics in the familial hypertrophic cardiomyopathy D166V mutant mouse heart.Journal of molecular and cellular cardiology · 2010Article
- Fluorescence applications in molecular neurobiology.Neuron · 2010Review
- The molecular effects of skeletal muscle myosin regulatory light chain phosphorylation.American journal of physiology. Regulatory, integrative and comparative physiology · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To study the orientation and dynamics of myosin, we measured fluorescence polarization of single molecules and ensembles of myosin decorating actin filaments. Engineered chicken gizzard regulatory light chain (RLC), labeled with bisiodoacetamidorhodamine at cysteine residues 100 and 108 or 104 and 115, was exchanged for endogenous RLC in rabbit skeletal muscle HMM or S1. AEDANS-labeled actin, fully decorated with labeled myosin fragment or a ratio of approximately 1:1000 labeled:unlabeled myosin fragment, was adhered to a quartz slide. Eight polarized fluorescence intensities were combined with the actin orientation from the AEDANS fluorescence to determine the axial angle (relative to actin), the azimuthal angle (around actin), and RLC mobility on the <<10 ms timescale. Order parameters of the orientation distributions from heavily labeled filaments agree well with comparable measurements in muscle fibers, verifying the technique. Experiments with HMM provide sufficient angular resolution to detect two orientations corresponding to the two heads in rigor. Experiments with S1 show a single orientation intermediate to the two seen for HMM. The angles measured for HMM are consistent with heads bound on adjacent actin monomers of a filament, under strain, similar to predictions based on ensemble measurements made on muscle fibers with electron microscopy and spectroscopic experiments.
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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.