3P115 High stability of two-dimensional crystal of reconstituted bacteriorhodopsin in partially fluorinated phosphatidylcholine(03. Membrane proteins,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))
Masaru Yoshino, Hiroshi Takahashi, K. Morita, T. Takagi, H. Amii, T. Kanamori, M. Sonoyama
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Abstract
We have reported successful reconstitution of bacteriorhodopsin (bR) into novel partially fluorinated phosphatidylcholine (diF4H10-PC) vesicles, in that the reconstituted bR has native-like higher order structure and photocycle. The present study on structural stability of the reconstituted bR demonstrated that 2D crystals as well as trimeric structure of bR molecules are maintained and no light-induced denaturation is observed up to ~40 °C, which is much higher than the gel-to-liquid crystalline phase transition temperature (5 °C) of pure diF4H10-PC bilayer. The high stability of the reconstituted bR in diF4H10-PC is in stark contrast with bR in DMPC showing phase transition-induced disassembly of bR molecules and remarkable denaturation by visible light.
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