Hydrophobicity analysis

Fig. 13.5. Hydrophobicity analysis of the predicted amino acid sequence from a metalloprotease component of H-gal-GP (MEP3) showing two potential transmembrane domains (indicated by open arrows). B41 and B47 indicate the relative positions of two N-terminal sequences determined from bands present when H-gal-GP is reduced.

Figure 14. Hydrophobicity analysis of five P-type ATPases according to the Kyte-Doolittle method. A hydrophobicity value between -4.5 and +4.5 is assigned to each type of amino acid residue and mean values are successively calculated along the peptide sequence using a window of 18 residues. Segments corresponding to the transmembrane helices M1-M10 in the structural model in Figure 15 are shaded. Modified from Verma et al., 1988.

G. von Heijne, Membrane protein structure prediction. Hydrophobicity analysis and the positive- inside rule, /. Mol. Biol. 225, 487 94 (1992). 

Lemesle-Varloot, L., Henrissat, B., Gaboriaud, C., Bissery, V., Morgat, A. Mornon, J.P. (1990) Biochimie, 72, 555-574. Hydrophobic analysis procedures to drive structural and functional information from 2-D-representation of protein sequences. 

Fig. 1. Structural organization of the human TAP complex. The membrane helices are predicted from hydrophobicity analysis and sequence alignment with MDRl. (Abele and Tampe 1999 Lankat-Butt-GEREIT and Tampe 1999). The N-terminal domain (N) comprises four and three transmembrane helices (TM), respectively. According to the 2 x 6 transmembrane helix model, the transmembrane helices are numbered TMl to TM6. The nucleotide-binding domains (NBDs) consist of the highly conserved Walker A and B motifs (A, B). The striped lines illustrate the peptide-binding region mapped by photo-crosslinking studies. (Nijenhuis and Hammerling 1996)...

Pyka, A. Vitamins, hydrophobic, analysis by thin layer chromatography. In On-line Sipplement of Encyclopedia of Chromatograph, 2nd Ed. Gazes, J., Ed. Taylor Francis, Inc. New York, 2006 1 1, 1-9. DOI 10.1081/E-ECHR-120042974 http //dx.doi.org/10.108 l/E-ECHR-120042974... 

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