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Protein Hydrophilicity Plot

A hydrophilicity plot is a quantitative analysis of the degree of hydrophobicity or hydrophilicity of amino acids of a protein. It is used to characterize or identify possible structure or domains of a protein.

The plot has amino acid sequence of a protein on its x-axis, and degree of hydrophobicity and hydrophilicity on its y-axis. There is a number of methods to measure the degree of interaction of polar solvents such as water with specific amino acids. For instance, the Kyte-Doolittle scale1 indicates hydrophobic amino acids(employed in this tool), whereas the Hopp-Woods scale measures hydrophilic residues.

1. Sequence (Paste the raw sequence, not fasta format):

Full length:0

Amino Acid Hydropathy Scores

Amino Acid One Letter Code Hydropathy Score
Isoleucine I 4.5
Valine V 4.2
Leucine L 3.8
Phenylalanine F 2.8
Cysteine C 2.5
Methionine M 1.9
Alanine A 1.8
Glycine G -0.4
Threonine T -0.7
Serine S -0.8
Tryptophan W -0.9
Tyrosine Y -1.3
Proline P -1.6
Histidine H -3.2
Glutamic acid E -3.5
Glutamine Q -3.5
Aspartic acid D -3.5
Asparagine N -3.5
Lysine K -3.9
Arginine R -4.5


The windows size is set to 9 aa. And weights for window positions 1,..,9, using linear weight variation model:

1 2 3 4 5 6 7 8 9
1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00
edge center edge


  • 1. Kyte, J; Doolittle, R. F. (1982). "A simple method for displaying the hydropathic character of a protein". Journal of Molecular Biology. 157 (1): 105–32.