ArticleBiophysical journal1996
Radial equilibrium lengths of actomyosin cross-bridges in muscle.
Article in Biophysical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Structural and functional impact of troponin C-mediated CaJournal of molecular and cellular cardiology · 2018Article
- Radial stability of the actomyosin filament lattice in isolated skeletal myofibrils studied using atomic force microscopy.The journal of physiological sciences : JPS · 2013Article
- An electrostatic model with weak actin-myosin attachment resolves problems with the lattice stability of skeletal muscle.Biophysical journal · 2011Article
- Regulatory light chain phosphorylation and N-terminal extension increase cross-bridge binding and power output in Drosophila at in vivo myofilament lattice spacing.Biophysical journal · 2011Article
- Impaired organization and function of myofilaments in single muscle fibers from a mouse model of Pompe disease.Journal of applied physiology (Bethesda, Md. : 1985) · 2010Article
- The effects of force inhibition by sodium vanadate on cross-bridge binding, force redevelopment, and Ca2+ activation in cardiac muscle.Biophysical journal · 2007Article
- Contributions of stretch activation to length-dependent contraction in murine myocardium.The Journal of general physiology · 2006Article
- Response of equatorial x-ray reflections and stiffness to altered sarcomere length and myofilament lattice spacing in relaxed skinned cardiac muscle.Biophysical journal · 2004Article
- Cooperative regulation of myosin-actin interactions by a continuous flexible chain II: actin-tropomyosin-troponin and regulation by calcium.Biophysical journal · 2003Article
- Direct modeling of x-ray diffraction pattern from skeletal muscle in rigor.Biophysical journal · 2002Article
- Structural features of cross-bridges in isometrically contracting skeletal muscle.Biophysical journal · 2002Article
- Changes in myofibrillar structure and function produced by N-terminal deletion of the regulatory light chain in Drosophila.Journal of muscle research and cell motility · 2001Article
- Time-resolved X-ray diffraction by skinned skeletal muscle fibers during activation and shortening.Biophysical journal · 2001Article
- Light chain-dependent myosin structural dynamics in solution investigated by transient electrical birefringence.Biophysical journal · 1997Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Radial equilibrium lengths of the weakly attached, force-generating, and rigor cross-bridges are determined by recording their resistance to osmotic compression. Radial equilibrium length is the surface-to-surface distance between myosin and actin filaments at which attached cross-bridges are, on average, radially undistorted. We previously proposed that differences in the radial equilibrium length represent differences in the structure of the actomyosin cross-bridge. Until now the radial equilibrium length had only been determined for various strongly attached cross-bridge states and was found to be distinct for each state examined. In the present work, we demonstrate that weakly attached cross-bridges, in spite of their low affinity for actin, also exert elastic forces opposing osmotic compression, and they are characterized by a distinct radial equilibrium length (12.0 nm vs. 10.5 nm for force-generating and 13.0 nm for rigor cross-bridge). This suggests significant differences in the molecular structure of the attached cross-bridges under these conditions, e.g., differences in the shape of the myosin head or in the docking of the myosin to actin. Thus, the present finding supports our earlier conclusion that there is a structural change in the attached cross-bridge associated with the transition from a weakly bound configuration to the force-generating configuration. The implications for imposing spatial constraints on modeling actomyosin interaction in the filament lattice are discussed.
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