PMID: 7085614Jun 25, 1982Paper

Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures.

The Journal of Biological Chemistry
E London, H G Khorana


The denatured and renatured states of bacteriorhodopsin have been studied in detergents and lipid/detergent mixtures by using ultraviolet and visible light absorption spectroscopy, fluorescence spectroscopy, and circular dichroism. Upon solubilization in sodium dodecyl sulfate, bacteriorhodopsin undergoes denaturation with partial loss of the secondary structure and loss of retinal binding ability. In contrast, delipidated bacteriorhodopsin retains its native structure in deoxycholate and undergoes denaturation only on photobleaching, which results in a partial loss of the secondary structure. Native secondary structure spontaneously reforms upon addition of phospholipid/cholate mixtures to bacterio-opsin denatured in sodium dodecyl sulfate. Upon subsequent addition of retinal, up to 95% of the native chromophore (lambdamax = 550-560 nm) is restored. Renaturation also restores the characteristics of light and dark adaptation and tight retinal binding (Kb greater than 10(7) M-1). Renaturation of delipidated bacteriorhodopsin denatured in sodium dodecyl sulfate also occurs without phospholipid upon the addition of retinal and Triton X-100 or octyl glucoside. The equilibrium between monomeric and oligomeric states of bacteriorhodo...Continue Reading

Related Concepts

Deoxycholic Acid, Sodium Salt, 12beta-Isomer
Plasma Protein Binding Capacity
Protein Denaturation

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