Abstract
Myelin basic proteins from human, bovine, porcine, rabbit and chicken central nervous systems were examined in aqueous solutions by proton n.m.r. at 400 MHz. Species comparisons and other techniques led to assignments of resonances to specific amino-acid residues. Titration effects associated with aspartic-acid sidechains were effective in identifying adjacent residues. Nuclear Overhauser difference spectra showed that the reverse turn previously suggested for the conformation of an isolated encephalitogenic nonapeptide (guinea-pig determinant) occurred also in the protein, thus supporting the concept of a special low-energy conformation associated with biological activity. The central region of the protein contains methyl groups in aliphatic sidechains with resonances having chemical shifts characteristic of strong shielding effects, thus supporting the idea that less extended secondary and tertiary structures occur in this region.
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