Computer modeling of membrane-anchored cellular and viral proteins: organization and function.
1. Although secondary structure predictions are only 60% correct, the computer programs provide some idea as to peptide conformation. 2. The detection of hydrophobic domains in membrane-bound proteins allowed the identification of membrane insertional domains in the polypeptide. 3. A combination of computer analyses of protein conformation and the identification of functional domains in polypeptides must be substantiated by experimental data. 4. Computer analyses of membrane proteins may provide a theoretical approach to the selection and development of antibiotics capable of interfering with the insertion and function of viral proteins in cellular membranes.
Becker
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Department of Molecular Virology, Faculty of Medicine, Hebrew University, Jerusalem, Israel.
D000465:Algorithms; D000595:Amino Acid Sequence; D000954:Antigens, Surface; D003198:Computer Simulation; D008555:Melitten; D008565:Membrane Proteins; D008958:Models, Molecular; D011487:Protein Conformation; D011498:Protein Precursors; D018800:Thy-1 Antigens; D014764:Viral Proteins
D000954:Antigens, Surface; D008565:Membrane Proteins; D011498:Protein Precursors; D018800:Thy-1 Antigens; D014764:Viral Proteins; D008555:Melitten; C016694:prepromelittin