June 1, 1993The Journal of Cell BiologyOpen Access

Time-resolved electron microscopic analysis of the behavior of myosin heads on actin filaments after photolysis of caged ATP.

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Population

Actin and myosin subfragment 1 (S1) (100 microM each) in the presence of 5 mM caged ATP

Comparison

Photolysis of caged ATP vs Pre-photolysis state (strongly bound S1)

Design

Preclinical

Follow-up

200 ms

Authors

TFTakashi FunatsuHiroshima University EKEiji KonoHamamatsu University School of Medicine STShöichiro TsukitaHiroshima University

Discussion

Member takes

Implication

Suggests distinct weak-binding dynamics in myosin; leaves open functional impact on cardiac force generation.

Structured PICO

Population

Actin and myosin subfragment 1 (S1) (100 microM each) in the presence of 5 mM caged ATP

Intervention

Photolysis of caged ATP

Comparator

Pre-photolysis state (strongly bound S1)

Outcome

Conformational differences and attachment angles of S1 to actin filaments

Time-resolved electron microscopy reveals that weakly bound myosin heads have a broader distribution of attachment angles to actin filaments compared to strongly bound heads, without significant conformational changes.

Cite This Study

Funatsu et al. (1993) studied this question.

synapsesocial.com/papers/6a20a8369ca8a48788f36f18 https://doi.org/10.1083/jcb.121.5.1053

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Time-resolved electron microscopic analysis of the behavior of myosin heads on actin filaments after photolysis of caged ATP.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Time-resolved electron microscopic analysis of the behavior of myosin heads on actin filaments after photolysis of caged ATP.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider