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See detailProposition Of A 3-Dimensional Representation Of The Constitutive Protein Of The Hepatitis-B Surface-Antigen Particles
Sonveaux, N.; Ruysschaert, Jm.; Brasseur, Robert ULg

in Journal of Protein Chemistry (1995), 14(6), 477-86

Hepatitis B surface antigen particles are composed of the major viral envelope protein, the S protein, embedded into a lipid shell. The description of the folding of this protein within the particle ... [more ▼]

Hepatitis B surface antigen particles are composed of the major viral envelope protein, the S protein, embedded into a lipid shell. The description of the folding of this protein within the particle membrane could provide helpful information for replacing surface-exposed protein domains by foreign sequences without destabilizing the particle structure. Since the crystallization of the protein in its lipid environment remains inaccessible in the near future, alternative approaches had to be envisaged. We combine here the available experimental structural and topological data with a conformational procedure to identify membrane-associated domains of the HBsAg protein and to propose a three-dimensional description of their assembly within the particle membrane. The proposed protein structure is composed of four membrane-spanning helices and an amphipatic helix located on the inner surface membrane. The transmembrane helices are assembled into a highly hydrophobic complex in which no access to the water environment is allowed. The approach could be extended to other membrane-associated proteins. [less ▲]

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See detailStructure and orientation of apo B-100 peptides into a lipid bilayer.
Lins, Laurence ULg; Brasseur, Robert ULg; Rosseneu, M. et al

in Journal of Protein Chemistry (1994), 13(1), 77-88

Peptides corresponding to lipid binding domains of Apo B-100 were synthesized, purified, and incubated with dimyristoylphosphatidylcholine (DMPC) liposomes. The secondary structure of the apo B-100 ... [more ▼]

Peptides corresponding to lipid binding domains of Apo B-100 were synthesized, purified, and incubated with dimyristoylphosphatidylcholine (DMPC) liposomes. The secondary structure of the apo B-100 peptide-lipid complexes was evaluated by attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR). Those peptides belonging to the hydrophobic "core" domain of apo B-100 when associated with phospholipids were rich in beta sheet structure; a predominant alpha helical conformation was shown to be associated with one peptide located in a surface region of apo B-100. IR dichroic spectra revealed, in the case of the "core" peptides, that the beta sheet component is the only oriented structure with respect to the phospholipid acyl chains. This orientation of the beta sheet was recently found in LDL particles after proteolytic digestion by trypsin (Goormaghtigh, E., Cabiaux, V., De Meutter, J., Rosseneu, M., and Ruysschaert, J. M., 1993, Biochemistry 32, 6104-6110). Altogether, the data suggest that beta sheet, present in a high proportion in the native apo B-100, is probably another protein structure in addition to the amphipathic helix which strongly interacts with the lipid outer layer surrounding the LDL particle. [less ▲]

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