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cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases

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European Journal of Biochemistry

Wiley-Blackwell

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      [57] Sequencing end-labeled DNA with base-specific chemical cleavages

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        Analysis of membrane and surface protein sequences with the hydrophobic moment plot.

        An algorithm has been developed which identifies alpha-helices involved in the interactions of membrane proteins with lipid bilayers and which distinguishes them from helices in soluble proteins. The membrane-associated helices are then classified with the aid of the hydrophobic moment plot, on which the hydrophobic moment of each helix is plotted as a function of its hydrophobicity. The magnitude of hydrophobic moment measures the amphiphilicity of the helix (and hence its tendency to seek a surface between hydrophobic and hydrophilic phases), and the hydrophobicity measures its affinity for the membrane interior. Segments of membrane proteins in alpha-helices tend to fall in one of three regions of a hydrophobic moment plot: (1) monomeric transmembrane anchors (class I HLA transmembrane sequences) lie in the region of highest hydrophobicity and smallest hydrophobic moment; (2) helices presumed to be paired (such as the transmembrane M segments of surface immunoglobulins) and helices which are bundled together in membranes (such as bacteriorhodopsin) fall in the adjacent region with higher hydrophobic moment and smaller hydrophobicity; and (3) helices from surface-seeking proteins (such as melittin) fall in the region with still higher hydrophobic moment. alpha-Helices from globular proteins mainly fall in a region of lower mean hydrophobicity and hydrophobic moment. Application of these methods to the sequence of diphtheria toxin suggests four transmembrane helices and a surface-seeking helix in fragment B, the moiety known to have transmembrane function.
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          Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint

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            Author and article information

            Journal
            European Journal of Biochemistry
            Eur J Biochem
            Wiley-Blackwell
            0014-2956
            1432-1033
            March 1989
            March 1989
            : 180
            : 2
            : 479-484
            10.1111/j.1432-1033.1989.tb14671.x
            © 1989

            http://doi.wiley.com/10.1002/tdm_license_1.1

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