April 1, 1987European Journal of BiochemistryOpen Access

Evidence that the N-terminal region of A1-light chain of myosin interacts directly with the C-terminal region of actin. A proton magnetic resonance study

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Population

Myosin subfragment-1 (S1) light chain isoenzymes from rabbit fast muscle and actin complexes

Design

Preclinical

Authors

ITIan P. TrayerUniversity of Birmingham HTHylary R. TrayerUniversity of Birmingham BLBarry A. LevineSan Francisco State University

Discussion

Member takes

Implication

No immediate clinical implications; leaves open functional roles of A1-actin contacts in cardiac contractility.

Structured PICO

Population

Myosin subfragment-1 (S1) light chain isoenzymes from rabbit fast muscle and actin complexes

Intervention

Proton magnetic resonance (1H-NMR) spectroscopy with spin-labeling of Cys-374 residue of actin

Outcome

Direct interaction and spatial proximity between the N-terminal region of the A1-light chain and the C-terminal region of actinsurrogate

This basic science study demonstrates a direct structural interaction between the N-terminal region of the myosin A1-light chain and the C-terminal region of actin.

Cite This Study

Trayer et al. (1987) studied this question.

synapsesocial.com/papers/6a161622dca1af9bedbf958a https://doi.org/10.1111/j.1432-1033.1987.tb11019.x

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Bookmark

Evidence that the N-terminal region of A1-light chain of myosin interacts directly with the C-terminal region of actin. A proton magnetic resonance study

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Evidence that the N-terminal region of A1-light chain of myosin interacts directly with the C-terminal region of actin. A proton magnetic resonance study

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider