Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 391-394 |
| Number of pages | 4 |
| Journal | European Journal of Biochemistry |
| Volume | 121 |
| Issue number | 2 |
| Publication status | Published - 1 Jan 1982 |