ArticleProceedings of the National Academy of Sciences of the United States of America2011
Structural kinetics of myosin by transient time-resolved FRET.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- DNA binding and transposition activity of the Sleeping Beauty transposase: role of structural stability of the primary DNA-binding domain.Nucleic acids research · 2025Article
- Fluorescence lifetime-based assay reports structural changes in cardiac muscle mediated by effectors of contractile regulation.The Journal of general physiology · 2023Article
- Article
- Kinetics of protein-assisted nucleic acid interconversion monitored by transient time resolved fluorescence in microfluidic droplets.Nucleic acids research · 2021Article
- FRET and optical trapping reveal mechanisms of actin activation of the power stroke and phosphate release in myosin V.The Journal of biological chemistry · 2020Article
- Article
- Dilated cardiomyopathy mutation in the converter domain of human cardiac myosin alters motor activity and response to omecamtiv mecarbil.The Journal of biological chemistry · 2019Article
- Converter domain mutations in myosin alter structural kinetics and motor function.The Journal of biological chemistry · 2019Article
- Targeting protein-protein interactions for therapeutic discovery via FRET-based high-throughput screening in living cells.Scientific reports · 2018Article
- A dynamic mechanism for allosteric activation of Aurora kinase A by activation loop phosphorylation.eLife · 2018Article
- Combining Graphical and Analytical Methods with Molecular Simulations To Analyze Time-Resolved FRET Measurements of Labeled Macromolecules Accurately.The journal of physical chemistry. B · 2017Article
- Heart failure drug changes the mechanoenzymology of the cardiac myosin powerstroke.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Highly selective inhibition of myosin motors provides the basis of potential therapeutic application.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Macromolecular Crowding Modulates Actomyosin Kinetics.Biophysical journal · 2016Article
- Biological Nanomotors with a Revolution, Linear, or Rotation Motion Mechanism.Microbiology and molecular biology reviews : MMBR · 2016Review
- The structural kinetics of switch-1 and the neck linker explain the functions of kinesin-1 and Eg5.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Direct measurements of the coordination of lever arm swing and the catalytic cycle in myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Direct real-time detection of the structural and biochemical events in the myosin power stroke.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Mechanochemical tuning of myosin-I by the N-terminal region.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- High-resolution helix orientation in actin-bound myosin determined with a bifunctional spin label.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
For many proteins, especially for molecular motors and other enzymes, the functional mechanisms remain unsolved due to a gap between static structural data and kinetics. We have filled this gap by detecting structure and kinetics simultaneously. This structural kinetics experiment is made possible by a new technique, (TR)(2)FRET (transient time-resolved FRET), which resolves protein structural states on the submillisecond timescale during the transient phase of a biochemical reaction. (TR)(2)FRET is accomplished with a fluorescence instrument that uses a pulsed laser and direct waveform recording to acquire an accurate subnanosecond time-resolved fluorescence decay every 0.1 ms after stopped flow. To apply this method to myosin, we labeled the force-generating region site specifically with two probes, mixed rapidly with ATP to initiate the recovery stroke, and measured the interprobe distance by (TR)(2)FRET with high resolution in both space and time. We found that the relay helix bends during the recovery stroke, most of which occurs before ATP is hydrolyzed, and two structural states (relay helix straight and bent) are resolved in each nucleotide-bound biochemical state. Thus the structural transition of the force-generating region of myosin is only loosely coupled to the ATPase reaction, with conformational selection driving the motor mechanism.
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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.