July 7, 1998Proceedings of the National Academy of SciencesOpen Access

Myosin conformational states determined by single fluorophore polarization

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Population

Turkey gizzard smooth muscle myosin and actin in an in vitro motility assay.

Design

Preclinical

Authors

DWDavid M. WarshawUniversity of Vermont EHEric HayesOregon National Primate Research Center DGDonald P. GaffneyUniversity of Vermont

Discussion

Member takes

Implication

Provides foundational myosin kinetics data in animals; hypothesis-generating for targeted therapies but should not yet change practice.

Structured PICO

Population

Turkey gizzard smooth muscle myosin and actin in an in vitro motility assay.

Intervention

Fluorescent labeling of regulatory light chain with 6-IATR and observation via spot-confocal fluorescence microscope.

Outcome

Myosin light chain domain orientational states (polarization angle) and event durations at varying MgATP concentrations.

This basic science study provides direct real-time evidence that the myosin light chain domain undergoes a disordered to ordered transition when moving from a detached to an attached force-generating state.

Cite This Study

Warshaw et al. (1998) studied this question.

synapsesocial.com/papers/6a83634e045de365ce2d02c0 https://doi.org/10.1073/pnas.95.14.8034

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Myosin conformational states determined by single fluorophore polarization

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Myosin conformational states determined by single fluorophore polarization

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider