Spectroscopic assessment of secondary and tertiary structure in myelin basic protein

Myelin basic protein conformation and hydrophobicity, along with the protein's behavior in the presence of the fluorescent probe 6-(p-toluidino)-2-naphthalenesulfonate, have been studied by using Fourier transform infrared (FT-IR) and Raman spectroscopy. The FT-IR and Raman spectra provided compelling evidence for the presence of a small amount of beta structure, ca. 25%, in the aqueous solution and solid-state forms of myelin basic protein. The enhanced fluorescence and shift in the emission maximum of 6-(p-toluidino)-2-naphthalenesulfonate when bound to myelin basic protein are consistent with the presence of at least one hydrophobic region in the molecule. Loss of the fluorescence enhancement in the presence of denaturing agents indicates that native myelin basic protein has a folded structure in solution. All of the results provide support for conformational predictions derived from the application of Edmundson wheels to the primary structure.