ArticleBiophysical journal2000
Conformational selection during weak binding at the actin and myosin interface.
Article in Biophysical journal, 2000. 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, 31 citations in OpenAlex.
- Modulation of striated-muscle contractility by a high-affinity myosin-targeting peptide.Biophysical journal · 2025Article
- Cooperative & competitive binding of anti-myosin tail antibodies revealed by super-resolution microscopy.Archives of biochemistry and biophysics · 2023Article
- Dynamics of ATP-dependent and ATP-independent steppings of myosin-V on actin: catch-bond characteristics.Journal of the Royal Society, Interface · 2020Article
- Single molecule mechanics resolves the earliest events in force generation by cardiac myosin.eLife · 2019Article
- A model for the chemomechanical coupling of myosin-V molecular motors.RSC advances · 2019Article
- ArabidopsisPlant physiology · 2018Article
- Structural basis for the in situ Ca(2+) sensitization of cardiac troponin C by positive feedback from force-generating myosin cross-bridges.Archives of biochemistry and biophysics · 2013Article
- Asymmetric myosin binding to the thin filament as revealed by a fluorescent nanocircuit.Archives of biochemistry and biophysics · 2013Article
- Demonstrating the uses of the novel gravitational force spectrometer to stretch and measure fibrous proteins.Journal of visualized experiments : JoVE · 2011Article
- The role of dynamic conformational ensembles in biomolecular recognition.Nature chemical biology · 2009Review
- Close proximity of myosin loop 3 to troponin determined by triangulation of resonance energy transfer distance measurements.Biochemistry · 2009Article
- Unconstrained steps of myosin VI appear longest among known molecular motors.Biophysical journal · 2004Article
- 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
- Mechanistic analysis of actin-binding compounds that affect the kinetics of cardiac myosin-actin interaction.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The molecular mechanism of the powerstroke in muscle is examined by resonance energy transfer techniques. Recent models suggesting a pre-cocking of the myosin head involving an enormous rotation between the lever arm and the catalytic domain were tested by measuring separation distances among myosin subfragment-2, the nucleotide site, and the regulatory light chain in the presence of nucleotide transition state analogs. Only small changes (<0.5 nm) were detected that are consistent with internal conformational changes of the myosin molecule, but not with extreme differences in the average lever arm position suggested by some atomic models. These results were confirmed by stopped-flow resonance energy transfer measurements during single ATP turnovers on myosin. To examine the participation of actin in the powerstroke process, resonance energy transfer between the regulatory light chain on myosin subfragment-1 and the C-terminus of actin was measured in the presence of nucleotide transition state analogs. The efficiency of energy transfer was much greater in the presence of ADP-AlF(4), ADP-BeF(x), and ADP-vanadate than in the presence of ADP or no nucleotide. These data detect profound differences in the conformations of the weakly and strongly attached cross-bridges that appear to result from a conformational selection that occurs during the weak binding of the myosin head to actin.
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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.