Myelin basic protein (MBP) has not been crystallized so has not been experimentally studied for its secondary and tertiary structure. As it appears to be involved in such demyelinating diseases as multiple sclorisis, this lack of knowledge of all but the primary structure hinders an understanding of its cause and ultimate treatment. This study proposes to examine this structure using force field methods to either support or refute an earlier proposal that MBP contains considerable structure counter to even earlier suggestions that MBP has a relatively open, flexible, and extended conformation. To obtain the minimum surface for MBP the program ECEPP83 will be used. The study will begin with the peptide 87-118. This peptide contains two strands of a beta-sheet and a hairpin loop that contains the rare triproline sequence of a previously proposed structure of MBP. Because the program restricts the phi angle of proline, several potential confomers will be examined. The peptide 37-95 will aso be examined. It is believed that these studies will support or refute the proposed structure of MBP and will be helpful in future studies of demyelinating diseases.
