Calculate hydrophobicity profile and hydrophobic/hydrophilic properties of protein and peptide sequences using amino acid hydrophobicity scales.
Average Hydrophobicity
--
Sequence Length
--
Hydrophobic Residues
--
Hydrophilic Residues
--
Maximum Hydrophobicity
--
Minimum Hydrophobicity
--
Hydrophobic Percentage
--
Protein hydrophobicity measures the tendency of amino acid residues to avoid water. It's crucial for understanding protein folding, membrane interactions, and biological activity.
Kyte-Doolittle is the most commonly used scale for general analysis. Eisenberg is good for membrane proteins, while Hopp-Woods is useful for predicting surface accessibility.
Window size determines the number of adjacent residues used to calculate the hydrophobicity profile. Larger windows provide smoother profiles, while smaller windows show more detail.
Terminal modifications can significantly alter the overall hydrophobicity of short peptides by adding hydrophobic or hydrophilic groups that change the molecule's properties.
Hydrophobic: F, I, L, M, V, W, Y, A. Hydrophilic: D, E, K, R, H, N, Q, S, T. Some amino acids like G, P, C have intermediate properties depending on the scale used.
Yes, this calculator works for both short peptides and long protein sequences. The analysis methods are the same, though interpretation may differ based on sequence length.
Use standard single-letter amino acid codes (A, C, D, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, Y). Spaces and line breaks are automatically removed.
The profile is calculated using a sliding window approach where the average hydrophobicity of residues within each window is computed and plotted against sequence position.