Related Experiment Video
Updated: Jun 7, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
Published on: November 30, 2018
Atomic force microscopy study of the rabbit skeletal muscle ryanodine receptors in different functional states
Qingqing Wei1, Xiaoyang Cheng, Keying Chen
1Laboratory of Neurobiology, Shanghai Institute of Physiology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 200031, Shanghai, China.
Abstract:
Atomic force microscope was applied to investigate the effect of extrinsic phospholipid on the structure of rabbit skeletal muscle ryanodine receptor/calcium release channel (RyR1). In addition, in the presence of extrinsic phospholipid, the height and elasticity of the RyR1s in different functional states were also measured. The results indicate: (i) most of the RyR1s showed a normal structure only in the presence of extrinsic phospholipid; (ii) treatment of the RyR1s with AMP and Ca(2+) together could increase their Young's Modulus but not change their apparent height; (iii) no detectable change in either height or Young's Modulus of the RyR1s appeared, if the RyR1s were treated with other activators or inhibitors.

