Figure 1
Structure prediction plots of CapZ alpha-subunit (residues 1–286) using matrix analyses according to Tempel et al. [10]. (A) Hydrophobicity, (B) Hydrophobic moment and (C) Probability of residues for CapZ alpha-subunit. Secondary structures (D) were calculated according to Eisenberg et al. [11] using a window of 11 residues. The secondary structure analyses of 113–130 (ADGGLKSWRESCDSALRA) and 225–242 (KEFIKIIENAENEYQTAI) are shown in (E) and (F), respectively. The two methods were carried out as follows: The 1st method relies only on the average amino acid composition of secondary structural segments (helix, sheet, coil) in a learning set of proteins, which showed an alpha-content of 55.2%, beta-content of zero, and a coil-content of 44.8% for (E); and an alpha-content of 100% and beta- and coil-contents of zero for (F). The 2nd method relies on composition fluctuations in the secondary structural segments (helix, sheet, coil) of a learning set of proteins, which showed an alpha-content of 38.1%, a beta-content of zero, and a coil-content of 61.9% for (E); and an alpha-content of 93.8%, a beta-content of 6.2%, and coil-content of zero for (F) [27-28].