Conformation of bovine myelin basic protein purified with bound lipids

The basic protein of myelin (called MBP) is an extrinsic protein of the mye lin membrane. Its structure and function are still unknown. MBP has been ex tensively studied in its water-soluble form, but it is also known in a dete rgent-soluble form, which is purified with endogenous myelin lipids and sho uld correspond to the native form of the protein in the membrane. In order to acquire insight into the structure of MBP, we have carried out circular dichroism (CD) experiments on the protein both in the lipid-free and in the lipid-bound form. Our data clearly show that lipid-free MBP is mainly diso rdered with only a small amount having alpha-helix and beta-sheet motifs. O n the other hand, the lipid-bound form of MBP appears to have a consistent amount of ordered secondary structure. Theoretical predictions, made using different computational methods, substantially confirm the tendency of the protein to assume an ordered secondary structure in accordance with our CD results.