部分氟化磷脂酰胆碱中重组菌紫质二维晶体的高稳定性[j]。膜蛋白，海报，第52届日本生物物理学会年会(BSJ2014)

Seibutsu Butsuri Pub Date : 2014-08-20 DOI:10.2142/biophys.54.S268_1

Masaru Yoshino, Hiroshi Takahashi, K. Morita, T. Takagi, H. Amii, T. Kanamori, M. Sonoyama

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摘要

我们已经成功地将细菌紫质(bR)重组成新的部分氟化磷脂酰胆碱(diF4H10-PC)囊泡，因为重组的bR具有类似天然的高阶结构和光循环。本研究对重组bR的结构稳定性进行了研究，结果表明，在~40℃的温度下，bR分子保持了二维晶体和三聚体结构，没有发生光致变性，远高于纯diF4H10-PC双分子层的凝胶-液晶相变温度(5℃)。diF4H10-PC中bR的高稳定性与DMPC中的bR形成鲜明对比，在可见光下表现出bR分子的相变引起的分解和显著的变性。

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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))

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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