Key result
Fluorescence resonance energy transfer efficiency did not change appreciably upon removal of Ca2+ ions, suggesting the C-terminal region of tropomyosin does not shift significantly relative to actin.
Population
Reconstituted skeletal muscle thin filaments with mutant tropomyosin molecules and actin
Comparison
Removal of Ca2+ ions vs Presence of Ca2+ ions
Design
Preclinical
Authors
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Reconstituted filament data do not support Ca2+-dependent C-terminal tropomyosin repositioning; leaves open its role in cardiac thin filament regulation.
Fluorescence resonance energy transfer analysis suggests that the C-terminal region of tropomyosin does not shift significantly relative to actin on the reconstituted thin filament in response to changes in calcium concentration.
M. Miki (2004) studied this question. Mutant tropomyosin molecules with unique cysteine residues vs. Changes in Ca2+ concentration was evaluated on Positional change of the C-terminal region of tropomyosin relative to actin (measured by FRET transfer efficiency). Fluorescence resonance energy transfer efficiency did not change appreciably upon removal of Ca2+ ions, suggesting the C-terminal region of tropomyosin does not shift significantly relative to actin.
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