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Possible Hydrophobic Region in Myelin Basic Protein Consisting of an Orthogonally Packed β‐Sheet

Abstract: Theoretical analysis was carried out to determine how the ∼20% of β‐structure observed in the 18.5 kilodalton (kDa) myelin basic protein (MBP) could be organized into a relatively stable β‐sheet. The β‐sheet is presumed to consist of the five most hydrophobic segments of polypeptide chain, which have β‐structure potential. These correspond approximately to sequences 15–21, 37–45, 84–92, 106–112, and 148–154 (rabbit MBP sequence numbering) and constitute β‐strands a,b,c,d, and e, respectively. A number of constraints are imposed upon the sheet; e.g., it should have the same topology in all MBP forms (21.5, 18.5, 17, and 14 kDa); strande should lie at the sheet edge; strands b, c, and d should be ordered sequentially; the sheet formed by strands a, b, c, and d should be antiparallel; a maximum of the nonpolar surface area should be removed from the aqueous milieu; and charged side chains should be solvent‐accessible. On the basis of these constraints it is possible to propose six orthogonally packed β‐sheets having different topologies. If strand e is restricted to an antiparallel alignment, the number of different sheets is reduced to four. Each of these sheets can form a relatively compact hydrophobic globular region. Two of the strands (a and e) can undergo transitions to α‐helix without disrupting the structure of the remaining sheet bcd or producing major topologic rearrangements of the polypeptide chain.