A Fourier transform infrared spectroscopic study of the secondary structure of myelin basic protein in reconstituted myelin

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Journal Article
Biochemistry and Molecular Biology International, 1996, 38 (4), pp. 839 - 845
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The secondary structure of myelin basic protein (MBP) in reconstituted central nervous system myelin was studied using Fourier transform infrared (FTIR) spectroscopy. The spectra of the protein in aqueous solution and in the lipid environment were compared and notable differences were observed. It is proposed that there are significant differences in the conformation of the protein in the contrasting environments. Significant increases in both α-helical structure and β-structure were observed on reconstitution in myelin. The findings of this study also support the view that the presence of both α-helices and β-structure plays a important role in membrane proteins.
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