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Background on Hydrophobicity Plots


Hydrophobicity (or hydrophilicity) plots are designed to display the distribution of polar and apolar residues along a protein sequence. Most commonly, such analysis has the goal of predicting membrane-spanning segments (highly hydrophobic) or regions that are likely exposed on the surface of proteins (hydrophilic domains) and therefore potentially antigenic.

To generate data for a plot, the protein sequence is scanned with a moving window of some size. At each position, the mean hydrophobic index of the amino acids within the window is calculated and that value plotted as the midpoint of the window. Several scales of hydrophobicity have been developed, most of which were derived from experimental studies on partitioning of peptides in apolar and polar solvents. Two of the most commonly used hydrophobicity scales are incorporated into the Hydropathy program:

Hydrophobicity Scales
              Kyte-Doolittle  Hopp-Woods

Alanine             1.8          -0.5
Arginine           -4.5           3.0
Asparagine         -3.5           0.2
Aspartic acid      -3.5           3.0
Cysteine            2.5          -1.0
Glutamine          -3.5           0.2
Glutamic acid      -3.5           3.0
Glycine            -0.4           0.0
Histidine          -3.2          -0.5
Isoleucine          4.5          -1.8
Leucine             3.8          -1.8
Lysine             -3.9           3.0
Methionine          1.9          -1.3
Phenylalanine       2.8          -2.5
Proline            -1.6           0.0
Serine             -0.8           0.3
Threonine          -0.7          -0.4
Tryptophan         -0.9          -3.4
Tyrosine           -1.3          -2.3
Valine              4.2          -1.5

Return to: Protein Hydrophobicity Plots

References

Hoop TP and Woods KR: Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci USA 78:3824, 1981.

Kyte J and Doolittle RF: A simple method for displaying the hydropathic character of a protien. J Mol Biol 157:105, 1982.


Last updated on June 20, 1998
Please send comments and report any bugs, errors or inaccuracies to: rbowen@lamar.colostate.edu