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Hydrophobicity profile

FIGURE 10.2 2D map of a whole cell lysate (top) along with an illustration of the reproducibility of the p / versus hydrophobicity profiling technique (bottom) using the Beckman PF2D automated instrument and software. (See color plate.)... [Pg.227]

Another recent trend is to show the importance of hydrophobic profiles rather than molecular hydrophobicity. Giuliani et al. (2002) suggested nonlinear signal analysis methods in the elucidation of protein sequence-structure relationships. The major algorithm used for analyzing hydrophobicity sequences or profiles was recurrence quantification analysis (RQA), in which a recurrence plot depicted a single trajectory as a two-dimensional representation of experimental time-series data. Examples of the global properties used in this... [Pg.311]

Figure 11.5. ProtScale (ExPASy Proteomic Tools) output of hydrophobicity parameter. The hydrophobicity profile of cod alcohol dehydrogenase is generated with ProtScale using Eisenberg hydrophobic scale. The individual values for the 20 amino acids used in the profile are also listed in the report. Figure 11.5. ProtScale (ExPASy Proteomic Tools) output of hydrophobicity parameter. The hydrophobicity profile of cod alcohol dehydrogenase is generated with ProtScale using Eisenberg hydrophobic scale. The individual values for the 20 amino acids used in the profile are also listed in the report.
Search the Web site to predict transmembrane topology of rhodopsin with the following sequence and compare the membrane-spanning regions with the hydrophobicity profiles of ProScale... [Pg.229]

The hydrophobicity profile is a simple way to quantify the concentration of hydrophobic residues along the linear polypeptide chain (Rose Dworkin, 1989). The construction of the profiles depends on the choice of the hydrophobicity scale and the window size. The profile is computed by averaging the hydrophobicity scales of amino acid residues within... [Pg.72]

Cid H, Bunster M, Arriagada E, Campos M. Prediction of secondary structure of proteins by means of hydrophobicity profiles. FEBS Lett. 1982 150 247-254. [Pg.27]

Figure 16.22. Model of a Mammalian Glucose Transporter. The hydrophobicity profile of the protein indicates 12 transmembrane a helices. [From M. Muekler, C. Caruso, S. A. Baldwin, M. Panico, M. Blench, H. R. Morris, W. J. Allard, G. E. Lienhard, and H. F. Lodish. Science 229(1985) 941.]... Figure 16.22. Model of a Mammalian Glucose Transporter. The hydrophobicity profile of the protein indicates 12 transmembrane a helices. [From M. Muekler, C. Caruso, S. A. Baldwin, M. Panico, M. Blench, H. R. Morris, W. J. Allard, G. E. Lienhard, and H. F. Lodish. Science 229(1985) 941.]...
HPLC/FPLC Fractionation based on physico-chemical featmes of protem (rn.w., pi, hydrophobic profile). Preparative/analytical... [Pg.727]

Figure 14 Distribution of the potential sites of fixation of succinyl residues (lysine, serine, threonine, ) along the amino acid sequence of the constituent a- and /3-polypeptide chains of pea legumin (from Ref. 97) and hydrophobicity profiles determined according to Ref. 98. (From Ref. Figure 14 Distribution of the potential sites of fixation of succinyl residues (lysine, serine, threonine, ) along the amino acid sequence of the constituent a- and /3-polypeptide chains of pea legumin (from Ref. 97) and hydrophobicity profiles determined according to Ref. 98. (From Ref.
Pimentel-Filho NDJ, et al. Bovicin HC5 and nisin reduce Staphylococcus aureus adhesion to polystyrene and change the hydrophobicity profile and Gibbs free energy of adhesion. Int J Food Microbiol 2014 190 1-8. [Pg.160]

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