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. 2000 Apr;68(4):1946–1952. doi: 10.1128/iai.68.4.1946-1952.2000

FIG. 3.

FIG. 3

Hydrophobicity/hydrophilicity profile and sequence variation in VR4 encoded by msp1β(F2) or msp1β(F3). The profile was calculated using the Kyte-Doolittle method (14) over a sliding window of 17 amino acids for the full-length MSP1bF2 and -F3. Relatively hydrophobic and hydrophilic domains are, respectively, above and below the x axis. The VR4 of MSP1bF2 (left panel) is shown with the positions of the three stretches of variant-specific oligopeptides indicated by lines labeled A, B, and C. The VR4 of MSP1bF3 (right panel) is shown with the positions of its variant-specific oligopeptides indicated by B′ and C′. There is no counterpart of the A stretch in MSP1bF3, because there is a deletion relative to MSP1bF2. The position of the deletion is indicated by the arrow.