December 8, 1992Biochemistry

Molecular movements in the actomyosin complex: F-actin-promoted internal cross-linking of the 25- and 20-kDa heavy chain fragments of skeletal myosin subfragment 1

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Population

Skeletal myosin subfragment 1 (S-1) and F-actin

Comparison

Chemical cross-linking with m-maleimidobenzoic… vs S-1 without actin

Design

Preclinical

Authors

RBRaoul BertrandCentre National de la Recherche Scientifique JDJean DerancourtCentre National de la Recherche Scientifique RKRidha KassabCentre National de la Recherche Scientifique

Discussion

Member takes

Implication

Indicates actin-dependent myosin remodeling in vitro; leaves open relevance to cardiac contractility or therapeutic targeting.

Structured PICO

Population

Skeletal myosin subfragment 1 (S-1) and F-actin

Intervention

Chemical cross-linking with m-maleimidobenzoic acid N-hydroxysuccinimide ester (MBS)

Comparator

S-1 without actin

Outcome

Changes in the spatial relationship of strands in the NH2-terminal 25-kDa and COOH-terminal 20-kDa heavy chain fragments (conversion of 95-kDa heavy chain to 135-kDa species)surrogate

This basic science study demonstrates F-actin-promoted changes in the spatial relationship of heavy chain fragments of skeletal myosin subfragment 1.

Cite This Study

Bertrand et al. (1992) studied this question.

synapsesocial.com/papers/6a714283a528af2d65c3fe2f https://doi.org/10.1021/bi00163a035

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Molecular movements in the actomyosin complex: F-actin-promoted internal cross-linking of the 25- and 20-kDa heavy chain fragments of skeletal myosin subfragment 1

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Molecular movements in the actomyosin complex: F-actin-promoted internal cross-linking of the 25- and 20-kDa heavy chain fragments of skeletal myosin subfragment 1

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider