Predication of secondary structures and epitopes of fusion protein pp150/MDBP.
- Author:
Dadong GUO
1
;
Xueqin GAO
;
Jinxiang HAN
Author Information
1. Key Laboratory for Biotech-drugs, Ministry of Health Shandong Medicinal Biotechnology Centre, Ji'nan 250062, China.
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Binding Sites;
Cytomegalovirus;
chemistry;
Epitopes;
Humans;
Molecular Sequence Data;
Phosphoproteins;
chemistry;
immunology;
Protein Structure, Secondary;
Viral Fusion Proteins;
chemistry;
immunology;
Viral Matrix Proteins;
chemistry;
immunology
- From:
Journal of Biomedical Engineering
2007;24(5):1123-1127
- CountryChina
- Language:Chinese
-
Abstract:
The secondary structures of fusion protein pp150/MDBP, including alpha-helix, beta-sheet, turn regions, were analyzed by Garnier-Robson's and Chou-Fasman's methods; the antigenic epitopes of B cells were analysed by using hydrophilicity plot. The results showed that the fusion protein pp150/MDBP might have less alpha-helix, but be rich in beta-sheet and turn regions. The epitopes recognized by B cells may be at 7-56 amino acid residues or adjacent to 137-192 amino acid residues.
