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The dependence of pH and ionic strength of kinetic absorption spectroscopy of acetylated bacteriorhodopsin

The dependence of pH and ionic strength of kinetic absorption spectroscopy of acetylated bacteriorhodopsin
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摘要 Bacteriorhodopsin (bR) in purple membrane (PM) from H. Halobium is a light-drivenproton pump. Its seven transmembrane helices form an internal proton channel. Anall-trans retinal covalently links up via protonated Schiff base with K216 inside thechannel. Upon illumination, the retinal isomerization around the C<sub>13</sub>-C<sub>14</sub> double bond drivesprotons translocation through the channel from the cytoplasm into the medium, and
出处 《Chinese Science Bulletin》 SCIE EI CAS 1995年第18期1558-1561,共4页
基金 Project supported by the Key Foundation of Chinese Academy of Sciences.
关键词 BACTERIORHODOPSIN ACETYLATION surface CHARGE INTERMEDIATE M412. BACTERIORHODOPSIN ACETYLATION SURFACE CHARGE INTERMEDIATE M412
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