June 22, 2001Biochemistry

Independent Movement of the Regulatory and Catalytic Domains of Myosin Heads Revealed by Phosphorescence Anisotropy

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Population

Whole myosin and the myosin head, subfragment-1, selectively labeled with eosin-5-iodoacetamide on the…

Design

Preclinical

Authors

LBLouise J. BrownNorthumbria University NKNicholas KlonisFlorida State University WSWilliam H. SawyerBrigham and Women's Hospital

Discussion

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Implication

Hypothesis-generating for cardiac myosin mechanics; extends structural models but leaves human translation open.

Structured PICO

Population

Whole myosin and the myosin head, subfragment-1 (S1), selectively labeled with eosin-5-iodoacetamide on the catalytic domain (Cys 707) and on two sites on the regulatory domain (Cys 177 on the essential light chain and Cys 154 on the regulatory light chain)

Intervention

Measurement of phosphorescence anisotropy in soluble S1 and myosin, with and without F-actin, and in synthetic myosin filaments

Outcome

Inter- and intradomain flexibility of the myosin head (anisotropy values)surrogate

The study demonstrates the presence of a point of flexibility between the catalytic and regulatory domains of myosin heads, consistent with models of force generation.

Cite This Study

Brown et al. (2001) studied this question.

synapsesocial.com/papers/6a86daadd25f83eb4715493b https://doi.org/10.1021/bi010566f

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Independent Movement of the Regulatory and Catalytic Domains of Myosin Heads Revealed by Phosphorescence Anisotropy

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Independent Movement of the Regulatory and Catalytic Domains of Myosin Heads Revealed by Phosphorescence Anisotropy

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider