October 1, 1997Biochemistry

Perturbations of Functional Interactions with Myosin Induce Long-Range Allosteric and Cooperative Structural Changes in Actin

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Population

Actin filaments (F-actin) and myosin subfragment 1 (S1) in vitro model

Comparison

Structural perturbations: binding of antibody… vs Myosin subfragment 1 (S1) in a rigor complex

Design

Preclinical

Authors

EPEwa PróchniewiczUniversity of Minnesota DTDavid D. ThomasHeart Failure / Cardiomyopathy

Discussion

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Implication

Actin stabilization may inhibit actomyosin interactions; hypothesis-generating for modulating cardiac contractility, pending validation.

Structured PICO

Population

Actin filaments (F-actin) and myosin subfragment 1 (S1) in vitro model

Intervention

Structural perturbations: binding of antibody fragment Fab(1-7) against the first seven N-terminal residues and copolymerization with EDC-treated monomers (EDC-actin)

Comparator

Myosin subfragment 1 (S1) in a rigor complex

Outcome

Rotational motion of actin measured by time-resolved phosphorescence anisotropy (TPA) of erythrosin iodoacetamide (ErIA) attached to Cys 374 on actinsurrogate

Functional perturbations transform actin to a form resembling the rigor actomyosin complex, suggesting actomyosin interaction can be inhibited by stabilizing actin in a structural intermediate.

Cite This Study

Próchniewicz et al. (1997) studied this question.

synapsesocial.com/papers/6a8586bd159a1fb27a202811 https://doi.org/10.1021/bi971201r

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Perturbations of Functional Interactions with Myosin Induce Long-Range Allosteric and Cooperative Structural Changes in Actin

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Perturbations of Functional Interactions with Myosin Induce Long-Range Allosteric and Cooperative Structural Changes in Actin

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider