Journal of Biology ›› 2019, Vol. 36 ›› Issue (5): 25-.doi: 10.3969/j.issn.2095-1736.2019.05.025

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Analysis of the molecular structure and physicochemical property of human Ryanodine receptors

  

  1. School of Public Health, University of South China, Hengyang 421001, China
  • Online:2019-10-18 Published:2019-10-11

Abstract: Ryanodine receptor (RyR) is an important ligand-gated Ca2+ channel. It is of great significance to analyze the structure and physicochemical properties of RyR, so that we can understand its regulation mechanism. In this study, bioinformatics methods were used to analyze the three subtypes of RyR (RyRs). The results showed that RyRs were hydrophilic protein, which have transmembrane structure, phosphorylation sites, and a large number of α-helix, but no disulfide bonds. RyRs have protein bonding and ion channel activity, participate in ion transporting, and so on. The bioinformatics analysis provides an important reference for the mechanism research and biological experiment of RyR.

Key words: Ryanodine receptor, bioinformatics, protein structure, amino acids

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