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Figure 7.
FIGURE 7. Comparison of hPAP and hLIT. A, sequence
alignment of hPAP and hLIT (identity, 47%). The secondary
structures of hPAP are shown, and the trypsin cleavage site is
indicated by a red arrow. Residue numbers for hPAP are shown
above the sequences, and those for hLIT are below the sequences.
The electrostatic potentials of the molecule surface of hPAP (B)
and hLIT (D) are shown with a similar orientation. Negative
potentials are colored red, and positive potentials are blue.
The hydrophobic surfaces of hPAP (C) and hLIT (E) are also shown
with a similar orientation. The protein surface is shown in
green, and exposed hydrophobic residues (Ala, Val, Leu, Ile,
Pro, Phe, Tyr, and Trp) are in yellow.
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