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Studies on the Temperature Effect on Bacteriorhodopsin of Purple and Blue Membrane by Fluo

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Studies on the Temperature Effect on

Bacteriorhodopsin of Purple and Blue Membrane by Fluorescence and Absorption Spectroscopy

Lan-Ying CHENG; Yue ZHANG; Shi-Gui LIU; Kun-Sheng HU; Kang-Cheng RUAN

【期刊名称】《《生物化学与生物物理学报:英文版》》 【年(卷),期】2006(038)010

【摘要】Fluorescence and absorption spectra were used to study the temperature effect on the conformation of bacteriorhodopsin (bR) in the blue and purple membranes (termed as bRb and bRp respectively). The maximum emission wavelengths of tryptophan fluorescence in both proteins at room temperature are 340 nm, and the fluorescence quantum yield of bRb is about 1.4 fold higher than that of bRp.As temperature increases, the tryptophan fluorescence of bRb decreases, while the tryptophan fluorescence of bRp increases. The binding study of extrinsic fluorescent probe bis-ANS indicated that the probe can bind only to bRb, but not to bRp. These results suggest that significant structural difference existed between bRb and bRp. It was also found that both kinds of bR are highly thermal stable. The maximum wavelength of the protein fluorescence emission only shifted from 340 nm to 346 nm at 100 ℃. More interestingly, as temperature increased, the characteristic absorption peak of bRb at 605 nm decreased and a new absorption peak at 380 nm formed. The transition occurred at a

Studies on the Temperature Effect on Bacteriorhodopsin of Purple and Blue Membrane by Fluo

StudiesontheTemperatureEffectonBacteriorhodopsinofPurpleandBlueMembranebyFluorescenceandAbsorptionSpectroscopyLan-YingCHENG;YueZHANG;Shi-GuiLIU;Kun-ShengHU;Kan
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