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COVER: Molecular modeling of the apoC-III peptide comprising residues 15-33, to predict the significance of the naturally occurring apoC-III Ala23Thr mutation. Top: distribution of hydrophobic and hydrophilic residues along the peptide showing good segregation of the hydrophilic and hydrophobic residues, suggesting an amphipathic helix (N-terminus to the right; C-terminus to the left; Ala23 in blue). Middle and bottom: the molecular hydrophobicity potentials of apoC-III Ala23 and apoC-III Thr23, respectively (green, hydrophilic domains; orange, hydrophobic domains). The surfaces are cut with a plane to visualize the mutated residues (blue) identified by the arrow. (See Liu et al., p. 1760.)
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