Prediction of secondary structural elements in the phosphatidylcholine-transfer protein from bovine liver.

R. Akeroyd; J. A. Lenstra; J. Westerman; G. Vriend; K. W. Wirtz; L. L. van Deenen

Prediction of secondary structural elements in the phosphatidylcholine-transfer protein from bovine liver.

R. Akeroyd^*
, J. A. Lenstra
, J. Westerman
, G. Vriend
, K. W. Wirtz
, L. L. van Deenen

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

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

Cite this

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title = "Prediction of secondary structural elements in the phosphatidylcholine-transfer protein from bovine liver.",

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.",

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AU - Akeroyd, R.

AU - Lenstra, J. A.

AU - Westerman, J.

AU - Vriend, G.

AU - Wirtz, K. W.

AU - van Deenen, L. L.

PY - 1982/1/1

Y1 - 1982/1/1

N2 - 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.

AB - 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.

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M3 - Article

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SN - 0014-2956

VL - 121

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JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

IS - 2

ER -

Prediction of secondary structural elements in the phosphatidylcholine-transfer protein from bovine liver.

Abstract

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