January 1, 1992Journal of Molecular BiologyOpen Access

Transients in orientation of a fluorescent cross-bridge probe following photolysis of caged nucleotides in skeletal muscle fibres

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Population

Single glycerol-extracted fibres of rabbit psoas muscle labelled with iodoacetamidotetramethylrhodamine at…

Design

Preclinical

Authors

JTJonathan W. TannerHospital of the University of Pennsylvania DTDavid D. ThomasHeart Failure / Cardiomyopathy YGYale E. GoldmanHeart Failure / Cardiomyopathy

Discussion

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Implication

Challenges probe interpretations in myosin mechanics studies; leaves open nucleotide-dominant mechanisms for future validation.

Structured PICO

Population

Single glycerol-extracted fibres of rabbit psoas muscle labelled with iodoacetamidotetramethylrhodamine at Cys707 of the myosin heavy chain

Intervention

Laser pulse photolysis of caged ATP and caged ADP

Outcome

Tension and linear dichroism of the probessurrogate

The orientation of rhodamine probes on the myosin head reflects structural changes linked to nucleotide binding and release rather than cross-bridge rotation during force generation.

Cite This Study

Tanner et al. (1992) studied this question.

synapsesocial.com/papers/6a71432026a7f98052dda4b5 https://doi.org/10.1016/0022-2836(92)90725-y

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Transients in orientation of a fluorescent cross-bridge probe following photolysis of caged nucleotides in skeletal muscle fibres

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Transients in orientation of a fluorescent cross-bridge probe following photolysis of caged nucleotides in skeletal muscle fibres

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider