Prediction of secondary structural elements in the phosphatidylcholine-transfer protein from bovine liver.
Secondary structural elements of the phosphatidylcholine-transfer protein from bovine liver have been predicted from its primary structure with the aid of two computerized methods. The predicted alpha-helix and beta-strand content have been compared with the values derived from circular dichroism spectra. The hydrophobicity profile (Rose plot) of the protein indicated that the supposed lipid-binding site occurs in the most hydrophobic region. The predicted secondary structural elements have been folded in a tentative model of the protein molecule according to its hydrophobicity profile.
D000595:Amino Acid Sequence; D000727:Androgen-Binding Protein; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification*; D002417:Cattle; D008099:Liver / Q000378:metabolism*; D008958:Models, Molecular; D049294:Phospholipid Transfer Proteins; D011487:Protein Conformation
D000727:Androgen-Binding Protein; D002352:Carrier Proteins; D049294:Phospholipid Transfer Proteins