Abstract
The type 1 ryanodine receptor (RyR1) mediates excitation contraction coupling in skeletal muscle by releasing stored intracellular calcium in response to cellular depolarization. This 2.2 MDa homotetrameric protein is associated with numerous regulatory proteins that modulate its activity in vivo. Understanding the structure and conformational dynamics of this immense macromolecular complex is an enormous challenge in skeletal muscle biology. In this report, structural determinations of RyR1 were performed using Förster resonance energy transfer (FRET) measurements.
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