Amino acid sequence and secondary structural map of 18.5-kDa murine myelin basic protein.

<p>The protein is intrinsically-disordered in aqueous solution but has three distinct segments which have α-helical propensity as shown (α₁, α₂, α₃) <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0068175#pone.0068175-Libich1" target="_blank">[27]</a>. The sequence enclosed by the red rectangle represents the reference α₂-peptide investigated in this study. This region consist of residues which can form an amphipathic α-helix when associated with lipids (α₂), followed by a proline-rich region of the protein which adopts a left-handed poly-proline II structure (PPII, shown in purple) that is the probable SH3-ligand. Within this poly-proline structure are two mitogen-activated protein kinase sites at T92 and T95 <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0068175#pone.0068175-Harauz4" target="_blank">[22]</a>. The figure is modified from <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0068175#pone.0068175-Ahmed1" target="_blank">[49]</a>.