The prediction of the conformation of membrane proteins from the sequence of amino acids.
The methods of Chou & Fasman [Biochemistry (1974) 13, 211-222, 222-245] and of Lim [J. Mol. Biol. (1974)88, 857-872, 873-894] for predicting secondary structure from amino acid sequence have been applied to five predominantly helical membrane-associated peptides. The predictions from the method of Lim (1974a,b) are consistent with the experimental observations, whereas those from Chou & Fasman (1974a,b), although not inconsistent with alpha-helix, favour a beta-structure for several very hydrophobic regions. The results may be rationalized in terms of the effect of the solvent on the conformation of a polypeptide.
D000595:Amino Acid Sequence; D003090:Coliphages / Q000032:analysis; D004912:Erythrocytes; D008566:Membranes; D010455:Peptides / Q000032:analysis; D011487:Protein Conformation; D014764:Viral Proteins / Q000032:analysis
D010455:Peptides; D014764:Viral Proteins