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Peptide Hydrophobicity/Hydrophilicity Analysis:

Sequence:


Other Modification:



Amino Acids Reference :
Amino Acids with Hydrophobic Side Chain - Aliphatic

Alanine, Ala, A

Isoleucine, Ile, I

Leucine, Leu, L

Valine, Val, V
Amino Acids with Hydrophobic Side Chain - Aromatic

Phenylalanine, Phe, F

Tryptophan, Trp, W

Tyrosine, Tyr, Y
Amino Acids with Polar Neutral Side Chains

Asparagine, Asn, N

Cysteine, Cys, C

Glutamine, Gln, Q

Methionine, Met, M

Serine, Ser, S

Threonine, Thr, T
Amino Acids with Electricaly Charged Side Chains - Acidic

Aspartic acid, Asp, D

Glutamic acid, Glu, E
Amino Acids with Electricaly Charged Side Chains - Basic

Arginine, Arg, R

Histidine, His, H

Lysine, Lys, K
Unique Amino Acids

Glycine, Gly, G

Proline, Pro, P
Properties of Common Amino Acids
Hydrophobicity Index for Common Amino Acids
The hydrophobicity index is a measure of the relative hydrophobicity, or how soluble an amino acid is in water. In a protein, hydrophobic amino acids are likely to be found in the interior, whereas hydrophilic amino acids are likely to be in contact with the aqueous environment.

The values in the table below are normalized so that the most hydrophobic residue is given a value of 100 relative to glycine, which is considered neutral (0 value). The scales were extrapolated to residues which are more hydrophilic than glycine.
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