Skip to main content
Figure 2 | Theoretical Biology and Medical Modelling

Figure 2

From: CapZ-lipid membrane interactions: a computer analysis

Figure 2

Structure prediction plots for CapZ beta-subunit (residues 1–272) using matrix analyses according to Tempel et al. [10]. (A) Hydrophobicity, (B) Hydrophobic moment and (C) Probability of residues for CapZ beta-subunit. Secondary structures (D) were calculated according to Eisenberg et al. [11] using a window of 11 residues. The secondary structure analyses of 134–151 (IKKAGDGSKKIKGCWDSI) and 215–232 (RLVEDMENKIRSTLNEIY) 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 zero, beta-content of zero, and a coil-content of 100% for (E); and an alpha-content of 67.2% and beta-content of 32.8%, and coil-content 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 16.4%, a beta-content of zero, and a coil-content of 83.6% for (E); and an alpha-content of 100%, beta- and coil-contents of zero, for (F) [27-28].

Back to article page