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COVER: Fourier transformation of mean residue helical hydrophobic moment (contour color) versus residue rotation angle (y-axis, 0-180 degrees) along the amino acid sequence of chicken apolipoprotein A-IV (x-axis, residues 1-346). Contour colors correspond to mean hydrophobic moments: white, <4.4 kcal/mol; dark green, 4.5-5.9 kcal/mol; light green, 6.0-6.9 kcal/mol; yellow, 7.0-7.9 kcal/mol; red, >8.0 kcal/mol. Regions of a-helical structure are identified as a band of isolines running across the middle of the figure. b-Sheet and random coil structure are indicated by isolines near the top and bottom of the figure, respectively. The break in the predominant a-helical pattern toward the C-terminus could represent a molecular footprint of the evolution of apolipoprotein A-IV by elongation of an ancestral apolipoprotein A-I molecule. (See Weinberg et al., p. 1410.) 
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