Folding Pathways of Photoactive Proton Pump Bacteriorhodopsin: A detailed kinetic study involving stopflow spectroscopy to deci,Used

Folding Pathways of Photoactive Proton Pump Bacteriorhodopsin: A detailed kinetic study involving stopflow spectroscopy to deci,Used

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SKU: DADAX3838319435
Brand: LAP Lambert Academic Publishing
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Stopflow fluorescence and photodiode array spectroscopy, with a millisecond time resolution, are used here to investigate refolding kinetics of the photoactive proton pump bacteriorhodopsin in mixed DMPC/CHAPS micelles from a partially denatured state in SDS. The study suggests that both the apoprotein folding and subsequent binding of retinal chromophore likely proceed via distinct multiple parallel pathways to generate the native helical bundle. Taken together, these data should have profound implications on the mechanisms of folding of proteins within biological membranes.

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