Virtual Molecule: P0 Myelin Glycoprotein. I. Homology Modeling and Prediction of the Secondary and Tertiary Structure - Molecules: Nucleation, Aggregation and Crystallization - page 244

Fig. 5. Hydrophobicity and hydrophilicity profiles of P0 protein prepared using the
BioEdit tool. A and B profiles are calculated based on the Kyte and Doolittle (1982)
scale. C and D hydrophilicity profiles are calculated based on the hydrophilicity scale
derived from high-performance liquid chromatography peptide retention data (Parker
et al ., 1986). A and C profiles are prepared for window size = 13 (6 a.a. before analyzed
position, 6 a.a. after analyzed position: 6 + 6 + 1 = 13). B and D profiles are for window
size = 7 (3 + 3 + 1). The region between 138-148 positions discloses a strongly
hydrophobic profile. This region belongs to the transmembrane helix (see Figs. 6 and 8).
There is also a hydrophobic region between 190-195 residues.