Intrinsic fluorescence of a non-myelin apoproteolipid and evidence for the existence of conformational flexibility.
An extremely hydrophobic protein (Mr = 16000), which in its native form is only soluble in organic solvents and which differs from the myelin proteolipid (Mr = 24000), was purified to homogeneity. Intrinsic fluorescence studies on this apoproteolipid have revealed a large conformational flexibility. In the water-soluble form the emitting residues appear to be buried in a hydrophobic core while in organic solvents they are exposed to the external medium. Structural changes depending on the organic solvent are also observed. The emission characteristics of reconstituted proteoliposomes may be due to the formation of a membrane-linked complex between several proteolipid monomers.
Lux
B
B
Laboratoire de Biophysique, ERA CNRS 551, UER des Sciences Pharmaceutiques, Université Louis Pasteur, B.P. 10, 67048 Strasbourg Cedex, France.
Helynck
G
G
Trifilieff
E
E
Luu
B
B
Gerard
D
D