ArticleBiophysical journal2008
Structural dynamics of the actomyosin complex probed by a bifunctional spin label that cross-links SH1 and SH2.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 32 citations in OpenAlex.
- Capturing protein dynamics across timescales with site-directed spin labeling electron paramagnetic resonance spectroscopy.Current opinion in structural biology · 2025Review
- Structural Dynamics of Protein Interactions Using Site-Directed Spin Labeling of Cysteines to Measure Distances and Rotational Dynamics with EPR Spectroscopy.Applied magnetic resonance · 2024Article
- A Highly Ordered Nitroxide Side Chain for Distance Mapping and Monitoring Slow Structural Fluctuations in Proteins.Applied magnetic resonance · 2024Article
- ADisease models & mechanisms · 2017Article
- The use of the Rx spin label in orientation measurement on proteins, by EPR.Physical chemistry chemical physics : PCCP · 2016Article
- A bifunctional spin label reports the structural topology of phospholamban in magnetically-aligned bicelles.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2016Article
- 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
- A nucleotide-independent cyclic nitroxide label for monitoring segmental motions in nucleic acids.BMC biophysics · 2015Article
- Coupling of lever arm swing and biased Brownian motion in actomyosin.PLoS computational biology · 2014Article
- Electron paramagnetic resonance resolves effects of oxidative stress on muscle proteins.Exercise and sport sciences reviews · 2014Review
- Conformationally trapping the actin-binding cleft of myosin with a bifunctional spin label.The Journal of biological chemistry · 2013Article
- Expression of the inclusion body myopathy 3 mutation in Drosophila depresses myosin function and stability and recapitulates muscle inclusions and weakness.Molecular biology of the cell · 2012Article
- Three distinct actin-attached structural states of myosin in muscle fibers.Biophysical journal · 2012Article
- Structure and dynamics of a conformationally constrained nitroxide side chain and applications in EPR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Structural kinetics of myosin by transient time-resolved FRET.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Mechanistic role of movement and strain sensitivity in muscle contraction.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Site-directed spectroscopic probes of actomyosin structural dynamics.Annual review of biophysics · 2009Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
We have used a bifunctional spin label (BSL) to cross-link Cys(707) (SH1) and Cys(697) (SH2) in the catalytic domain of myosin subfragment 1 (S1). BSL induces the same weakened ATPase activity and actin-binding affinity that is observed when SH1 and SH2 are cross-linked with pPDM, which traps an analog of the post-hydrolysis state A.M.ADP.P. Electron paramagnetic resonance showed that BSL reports the global orientation and dynamics of S1. When bound to actin in oriented muscle fibers in the absence of ATP, BSL-S1 showed almost complete orientational disorder, as reported previously for the weakly bound A.M.ADP. In contrast, helical order is observed for the strongly bound state A.M. Saturation transfer electron paramagnetic resonance showed that the disorder of cross-linked S1 on actin is nearly static on the microsecond timescale, at least 30 times slower than that of A.M.ADP. We conclude that cross-linked S1 exhibits rotational disorder comparable to that of A.M.ADP, slow rotational mobility comparable to that of A.M, and intermediate actin affinity. These results support the hypothesis that the catalytic domain of myosin is orientationally disordered on actin in a post-hydrolysis state in the early stages of force generation.
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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.