Secondary structure of GPI attachment signal region monitored by circular dichroism

Yuri Ikeda, Daiki Takahashi, Keiya Inoue, Hiromu Sugita, Tatsuki Kikegawa, Kenji Etchuya

研究成果: Article

抜粋

Secondary structure of the glycosylphosphatidylinositol attachment signal (GPI-AS) in GPI-anchored proteins, usually cleaved from the mature protein in eukaryotic cells, was evaluated using circular dichroism (CD). GPI-AS was expressed in Escherichia coli and was purified as a green fluorescent protein (GFP)-fused recombinant protein. The secondary structure was monitored by observing the far-UV CD bands. The α-helix content increased by 3.7% (indicates 13 amino acids) in GFP-fused GPI-AS, indicating that GPI-AS tends to have an α-helical structure. The method we propose in this study can be used to evaluate the secondary structure of the signal regions, which are absent in the mammalian mature proteins.

元の言語English
ページ(範囲)1153-1155
ページ数3
ジャーナルChemistry Letters
45
発行部数10
DOI
出版物ステータスPublished - 1 1 2016

これを引用

Ikeda, Y., Takahashi, D., Inoue, K., Sugita, H., Kikegawa, T., & Etchuya, K. (2016). Secondary structure of GPI attachment signal region monitored by circular dichroism. Chemistry Letters, 45(10), 1153-1155. https://doi.org/10.1246/cl.160551