Hydropathy Calculator
Compare the overall hydropathy of a peptide or protein with local changes along its sequence. The whole-sequence mean summarizes the sequence, while the sliding profile helps locate stretches with higher or lower Kyte–Doolittle scores. Adjust the window to see how smoothing affects the profile.
Results
Enter a valid sequence to calculate average hydropathy and plot its sliding-window profile.
How hydropathy is calculated
Average the Kyte–Doolittle scores across the whole sequence for GRAVY. Move a window one residue at a time and plot the mean of each complete window at its center. The default window is 9 residues or the full length for shorter sequences.
Read the calculation method →Worked example
VVVLLLDDDKKK
The whole-sequence average is 0.1500. With the default 9-residue window, the first window averages 1.5000 and the last averages −1.2000.
Limitations
- Scores are unitless. Positive scores indicate more hydrophobic character on this scale, while negative scores indicate more hydrophilic character.
- Profile shape depends on window size. Hydropathy alone cannot establish membrane topology or protein structure.