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. 1979 Mar;25(3):473–487. doi: 10.1016/S0006-3495(79)85317-5

Polarized infrared spectroscopy of oriented purple membrane.

K J Rothschild, N A Clark
PMCID: PMC1328485  PMID: 262400

Abstract

Polarized Fourier transform infrared spectroscopy has been used to study the structure of purple membrane from Halobacterium halobium. Membranes were oriented by drying a suspension of membrane fragments onto Irtran-4 slides. Dichroism measurements of the amide I, II and A peaks were used to find the average spatial orientation of the bacteriorhodopsin alpha-helices. By deriving a function that relates the observed dichroism to the orientational order parameters for the peptide groups, helical axis distribution, and mosaic spread of the membranes, the average orientation of the alpha-helices was found to lie in a range of less than 26 degrees away from the membrane normal, agreeing with electron microscopic measurements. The frequency of the amide I and A peaks is at least 10 cm-1 higher than values found for most alpha-helical polypeptides and proteins. This may indicate that bacteriorhodopsin contains distorted alpha-helical conformations.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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