Prediction of Secondary Structura1 Elements in the Phosphatidylcholine–Transfer Protein from Bovine Liver

Abstract
Secondary structural elements of the phosphatidylcholine-transfer protein from bovine liver were predicted from its primary structure with the aid of 2 computerized methods. The predicted .alpha.-helix and .beta.-strand content were 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 were folded in a tentative model of the protein molecule according to its hydrophobicity profile.

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