ArticleBiophysical journal1998
Luminescence resonance energy transfer measurements in myosin.
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 14 papers.
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Who cites it
14 citing papers in PubMed, 44 citations in OpenAlex.
- Fluorescence anisotropy of protein complexes in living cells.Biophysical journal · 2010Article
- Fluorescence applications in molecular neurobiology.Neuron · 2010Review
- Short-distance probes for protein backbone structure based on energy transfer between bimane and transition metal ions.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Close proximity of myosin loop 3 to troponin determined by triangulation of resonance energy transfer distance measurements.Biochemistry · 2009Article
- Site-directed spectroscopic probes of actomyosin structural dynamics.Annual review of biophysics · 2009Review
- Use of a novel Förster resonance energy transfer method to identify locations of site-bound metal ions in the U2-U6 snRNA complex.Nucleic acids research · 2007Article
- Effects of Metallic Silver Particles on Resonance Energy Transfer Between Fluorophores Bound to DNA.Journal of fluorescence · 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
- The elementary force generation process probed by temperature and length perturbations in muscle fibres from the rabbit.The Journal of physiology · 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
- Engineering a terbium-binding site into an integral membrane protein for luminescence energy transfer.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Conformational selection during weak binding at the actin and myosin interface.Biophysical journal · 2000Article
- Mechanics and models of the myosin motor.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2000Review
- Conformational changes between the active-site and regulatory light chain of myosin as determined by luminescence resonance energy transfer: the effect of nucleotides and actin.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Myosin is thought to generate force by a rotation between the relative orientations of two domains. Direct measurements of distances between the domains could potentially confirm and quantify these conformational changes, but efforts have been hampered by the large distances involved. Here we show that luminescence resonance energy transfer (LRET), which uses a luminescent lanthanide as the energy-transfer donor, is capable of measuring these long distances. Specifically, we measure distances between the catalytic domain (Cys707) and regulatory light chain domain (Cys108) of the myosin head. An energy transfer efficiency of 21.2 +/- 1.9% is measured in the myosin complex without nucleotide or actin, corresponding to a distance of 73 A, consistent with the crystal structure of Rayment et al. Upon binding to actin, the energy transfer efficiency decreases by 4.5 +/- 1.0%, indicating a conformational change in myosin that involves a relative rotation and/or translation of Cys707 relative to the light chain domain. Addition of ADP also alters the energy transfer efficiency, likely through a rotation of the probe attached to Cys707. These results demonstrate that LRET is capable of making accurate measurements on the relatively large actomyosin complex, and is capable of detecting conformational changes between the catalytic and light chain domains of myosin.
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