Abstract
Fourier transform infrared spectroscopy is used to estimate the secondary structure of bacteriorhodopsin dissolved in Chloroform-methanol (1:1 v v ), 0.1 M LiClO 4. Curve-fitting of the deconvolved spectra in the amide I region shows that the total content of α-helices, reverse turns and β-sheets are similar to the native state. However, the α II-helices, which are the major helical class in native bacteriorhodopsin, are greatly decreased in the solubilized sample. Similarly, the reverse turns and the β-sheets are strongly altered.
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